Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme

Dierks T, Dickmanns A, Preusser-Kunze A, Schmidt B, Mariappan M, Figura von K, Ficner R, Rudolph MG (2005)
CELL 121(4): 541-552.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate.
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CELL
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121
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4
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541-552
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Dierks T, Dickmanns A, Preusser-Kunze A, et al. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL. 2005;121(4):541-552.
Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., Figura von, K., Ficner, R., et al. (2005). Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL, 121(4), 541-552. doi:10.1016/j.cell.2005.03.001
Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., Figura von, K., Ficner, R., and Rudolph, M. G. (2005). Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL 121, 541-552.
Dierks, T., et al., 2005. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL, 121(4), p 541-552.
T. Dierks, et al., “Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme”, CELL, vol. 121, 2005, pp. 541-552.
Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., Figura von, K., Ficner, R., Rudolph, M.G.: Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL. 121, 541-552 (2005).
Dierks, Thomas, Dickmanns, A, Preusser-Kunze, A, Schmidt, B, Mariappan, M, Figura von, K, Ficner, R, and Rudolph, MG. “Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme”. CELL 121.4 (2005): 541-552.

84 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Expression, activity and localization of lysosomal sulfatases in Chronic Obstructive Pulmonary Disease.
Weidner J, Jogdand P, Jarenbäck L, Åberg I, Helihel D, Ankerst J, Westergren-Thorsson G, Bjermer L, Erjefält JS, Tufvesson E., Sci Rep 9(1), 2019
PMID: 30760748
How Are Proteins Reduced in the Endoplasmic Reticulum?
Ellgaard L, Sevier CS, Bulleid NJ., Trends Biochem Sci 43(1), 2018
PMID: 29153511
Neuro-ichthyotic Syndromes: A Case Series.
Incecık F, Herguner OM, Ozbek MN, Gungor S, Yılmaz M, Rizzo WB, Mert GG., J Pediatr Neurosci 13(1), 2018
PMID: 29899769
Copper is a Cofactor of the Formylglycine-Generating Enzyme.
Knop M, Dang TQ, Jeschke G, Seebeck FP., Chembiochem 18(2), 2017
PMID: 27862795
Crystal structure of PvdO from Pseudomonas aeruginosa.
Yuan Z, Gao F, Bai G, Xia H, Gu L, Xu S., Biochem Biophys Res Commun 484(1), 2017
PMID: 28109878
Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface.
Watanabe S, Harayama M, Kanemura S, Sitia R, Inaba K., Proc Natl Acad Sci U S A 114(16), 2017
PMID: 28373561
Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.
Waldman AJ, Ng TL, Wang P, Balskus EP., Chem Rev 117(8), 2017
PMID: 28375000
Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9.
Sun L, Chen P, Su Y, Cai Z, Ruan L, Xu X, Wu Y., Biosci Rep 37(3), 2017
PMID: 28442601
Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme.
Meury M, Knop M, Seebeck FP., Angew Chem Int Ed Engl 56(28), 2017
PMID: 28544744
1.8 Å resolution crystal structure of the carbapenem intrinsic resistance protein CarF.
Tichy EM, Hardwick SW, Luisi BF, Salmond GPC., Acta Crystallogr D Struct Biol 73(pt 7), 2017
PMID: 28695855
Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency.
Meshach Paul D, Chadah T, Senthilkumar B, Sethumadhavan R, Rajasekaran R., J Biomol Struct Dyn (), 2017
PMID: 29048999
Steroid Sulfatase Deficiency and Androgen Activation Before and After Puberty.
Idkowiak J, Taylor AE, Subtil S, O'Neil DM, Vijzelaar R, Dias RP, Amin R, Barrett TG, Shackleton CH, Kirk JM, Moss C, Arlt W., J Clin Endocrinol Metab 101(6), 2016
PMID: 27003302
Current Status: Site-Specific Antibody Drug Conjugates.
Schumacher D, Hackenberger CP, Leonhardt H, Helma J., J Clin Immunol 36 Suppl 1(), 2016
PMID: 27003914
Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway.
Goncharenko KV, Vit A, Blankenfeldt W, Seebeck FP., Angew Chem Int Ed Engl 54(9), 2015
PMID: 25597398
Natural disease history and characterisation of SUMF1 molecular defects in ten unrelated patients with multiple sulfatase deficiency.
Sabourdy F, Mourey L, Le Trionnaire E, Bednarek N, Caillaud C, Chaix Y, Delrue MA, Dusser A, Froissart R, Garnotel R, Guffon N, Megarbane A, Ogier de Baulny H, Pédespan JM, Pichard S, Valayannopoulos V, Verloes A, Levade T., Orphanet J Rare Dis 10(), 2015
PMID: 25885655
Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion.
Holder PG, Jones LC, Drake PM, Barfield RM, Bañas S, de Hart GW, Baker J, Rabuka D., J Biol Chem 290(25), 2015
PMID: 25931126
Orthogonal dual-modification of proteins for the engineering of multivalent protein scaffolds.
Mühlberg M, Hoesl MG, Kuehne C, Dernedde J, Budisa N, Hackenberger CPR., Beilstein J Org Chem 11(), 2015
PMID: 26124880
Human recombinant lysosomal enzymes produced in microorganisms.
Espejo-Mojica ÁJ, Alméciga-Díaz CJ, Rodríguez A, Mosquera Á, Díaz D, Beltrán L, Díaz S, Pimentel N, Moreno J, Sánchez J, Sánchez OF, Córdoba H, Poutou-Piñales RA, Barrera LA., Mol Genet Metab 116(1-2), 2015
PMID: 26071627
Eukaryotic formylglycine-generating enzyme catalyses a monooxygenase type of reaction.
Peng J, Alam S, Radhakrishnan K, Mariappan M, Rudolph MG, May C, Dierks T, von Figura K, Schmidt B., FEBS J 282(17), 2015
PMID: 26077311
Dealing with oxygen using bare hands.
Mattevi A., FEBS J 282(17), 2015
PMID: 26179614
In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I).
Knop M, Engi P, Lemnaru R, Seebeck FP., Chembiochem 16(15), 2015
PMID: 26403223
Effects of glycosylation and pH conditions in the dynamics of human arylsulfatase A.
Virgens MY, Pol-Fachin L, Verli H, Saraiva-Pereira ML., J Biomol Struct Dyn 32(4), 2014
PMID: 23581857
Chemical approaches to detect and analyze protein sulfenic acids.
Furdui CM, Poole LB., Mass Spectrom Rev 33(2), 2014
PMID: 24105931
Radical S-adenosylmethionine enzymes.
Broderick JB, Duffus BR, Duschene KS, Shepard EM., Chem Rev 114(8), 2014
PMID: 24476342
Chemoenzymatic Fc glycosylation via engineered aldehyde tags.
Smith EL, Giddens JP, Iavarone AT, Godula K, Wang LX, Bertozzi CR., Bioconjug Chem 25(4), 2014
PMID: 24702330
Molecular evaluation of a novel missense mutation & an insertional truncating mutation in SUMF1 gene.
Kotecha UH, Movva S, Sharma D, Verma J, Puri RD, Verma IC., Indian J Med Res 140(1), 2014
PMID: 25222778
Case of multiple sulfatase deficiency and ocular albinism: a diagnostic odyssey.
Prasad C, Rupar CA, Campbell C, Napier M, Ramsay D, Tay KY, Sharan S, Prasad AN., Can J Neurol Sci 41(5), 2014
PMID: 25373814
Proprotein convertases process and thereby inactivate formylglycine-generating enzyme.
Ennemann EC, Radhakrishnan K, Mariappan M, Wachs M, Pringle TH, Schmidt B, Dierks T., J Biol Chem 288(8), 2013
PMID: 23288839
Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency.
Schlotawa L, Radhakrishnan K, Baumgartner M, Schmid R, Schmidt B, Dierks T, Gärtner J., Eur J Hum Genet 21(9), 2013
PMID: 23321616
Effects of open versus laparoscopic nephrectomy techniques on oxidative stress markers in patients with renal cell carcinoma.
Mila-Kierzenkowska C, Woźniak A, Drewa T, Woźniak B, Szpinda M, Krzyżyńska-Malinowska E, Rajewski P., Oxid Med Cell Longev 2013(), 2013
PMID: 23533691
N-Terminal dual protein functionalization by strain-promoted alkyne-nitrone cycloaddition.
Temming RP, Eggermont L, van Eldijk MB, van Hest JC, van Delft FL., Org Biomol Chem 11(17), 2013
PMID: 23487244
Further characterization of Cys-type and Ser-type anaerobic sulfatase maturating enzymes suggests a commonality in the mechanism of catalysis.
Grove TL, Ahlum JH, Qin RM, Lanz ND, Radle MI, Krebs C, Booker SJ., Biochemistry 52(17), 2013
PMID: 23477283
X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification.
Goldman PJ, Grove TL, Sites LA, McLaughlin MI, Booker SJ, Drennan CL., Proc Natl Acad Sci U S A 110(21), 2013
PMID: 23650368
ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor.
Oka OB, Pringle MA, Schopp IM, Braakman I, Bulleid NJ., Mol Cell 50(6), 2013
PMID: 23769672
The structure of human α-2,6-sialyltransferase reveals the binding mode of complex glycans.
Kuhn B, Benz J, Greif M, Engel AM, Sobek H, Rudolph MG., Acta Crystallogr D Biol Crystallogr 69(pt 9), 2013
PMID: 23999306
Arylsulfatase K, a novel lysosomal sulfatase.
Wiegmann EM, Westendorf E, Kalus I, Pringle TH, Lübke T, Dierks T., J Biol Chem 288(42), 2013
PMID: 23986440
The cellular pathology of lysosomal diseases.
Cox TM, Cachón-González MB., J Pathol 226(2), 2012
PMID: 21990005
Recognition and diagnosis of neuro-ichthyotic syndromes.
Rizzo WB, Jenkens SM, Boucher P., Semin Neurol 32(1), 2012
PMID: 22422210
Synthesis of heterobifunctional protein fusions using copper-free click chemistry and the aldehyde tag.
Hudak JE, Barfield RM, de Hart GW, Grob P, Nogales E, Bertozzi CR, Rabuka D., Angew Chem Int Ed Engl 51(17), 2012
PMID: 22407566
Site-specific chemical protein conjugation using genetically encoded aldehyde tags.
Rabuka D, Rush JS, deHart GW, Wu P, Bertozzi CR., Nat Protoc 7(6), 2012
PMID: 22576105
Disulfide bond formation in the mammalian endoplasmic reticulum.
Bulleid NJ., Cold Spring Harb Perspect Biol 4(11), 2012
PMID: 23125019
SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency.
Schlotawa L, Ennemann EC, Radhakrishnan K, Schmidt B, Chakrapani A, Christen HJ, Moser H, Steinmann B, Dierks T, Gärtner J., Eur J Hum Genet 19(3), 2011
PMID: 21224894
Lysosomal lipid storage diseases.
Schulze H, Sandhoff K., Cold Spring Harb Perspect Biol 3(6), 2011
PMID: 21502308
HpSumf1 is involved in the activation of sulfatases responsible for regulation of skeletogenesis during sea urchin development.
Sakuma T, Ohnishi K, Fujita K, Ochiai H, Sakamoto N, Yamamoto T., Dev Genes Evol 221(3), 2011
PMID: 21706447
Cofactor-independent oxidases and oxygenases.
Fetzner S, Steiner RA., Appl Microbiol Biotechnol 86(3), 2010
PMID: 20157809
Protein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetASE/amidase in redox regulation.
Chiang BY, Chen TC, Pai CH, Chou CC, Chen HH, Ko TP, Hsu WH, Chang CY, Wu WF, Wang AH, Lin CH., J Biol Chem 285(33), 2010
PMID: 20530482
Sulf-2: an extracellular modulator of cell signaling and a cancer target candidate.
Rosen SD, Lemjabbar-Alaoui H., Expert Opin Ther Targets 14(9), 2010
PMID: 20629619
Neonatal manifestation of multiple sulfatase deficiency.
Busche A, Hennermann JB, Bürger F, Proquitté H, Dierks T, von Arnim-Baas A, Horn D., Eur J Pediatr 168(8), 2009
PMID: 19066960
Saposin B-dependent reconstitution of arylsulfatase A activity in vitro and in cell culture models of metachromatic leukodystrophy.
Matzner U, Breiden B, Schwarzmann G, Yaghootfam A, Fluharty AL, Hasilik A, Sandhoff K, Gieselmann V., J Biol Chem 284(14), 2009
PMID: 19224915
TagR promotes PpkA-catalysed type VI secretion activation in Pseudomonas aeruginosa.
Hsu F, Schwarz S, Mougous JD., Mol Microbiol 72(5), 2009
PMID: 19400797
Multiple sulfatase deficiency: clinical report and description of two novel mutations in a Brazilian patient.
Artigalás OA, da Silva LR, Burin M, Pastores GM, Zeng B, Macedo N, Schwartz IV., Metab Brain Dis 24(3), 2009
PMID: 19697114
Role of nitric oxide in regulating aldose reductase activation in the ischemic heart.
Kaiserova K, Tang XL, Srivastava S, Bhatnagar A., J Biol Chem 283(14), 2008
PMID: 18223294
Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals.
Gande SL, Mariappan M, Schmidt B, Pringle TH, von Figura K, Dierks T., FEBS J 275(6), 2008
PMID: 18266766
Treatment perspectives for the lysosomal storage diseases.
Grabowski GA., Expert Opin Emerg Drugs 13(1), 2008
PMID: 18321157
Function and structure of a prokaryotic formylglycine-generating enzyme.
Carlson BL, Ballister ER, Skordalakes E, King DS, Breidenbach MA, Gilmore SA, Berger JM, Bertozzi CR., J Biol Chem 283(29), 2008
PMID: 18390551
Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44.
Fraldi A, Zito E, Annunziata F, Lombardi A, Cozzolino M, Monti M, Spampanato C, Ballabio A, Pucci P, Sitia R, Cosma MP., Hum Mol Genet 17(17), 2008
PMID: 18508857
Chemoselective modification of proteins: hitting the target.
Carrico IS., Chem Soc Rev 37(7), 2008
PMID: 18568168
In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters.
Grove TL, Lee KH, St Clair J, Krebs C, Booker SJ., Biochemistry 47(28), 2008
PMID: 18558715
Sulfotransferases, sulfatases and formylglycine-generating enzymes: a sulfation fascination.
Bojarová P, Williams SJ., Curr Opin Chem Biol 12(5), 2008
PMID: 18625336
Partial cure of established disease in an animal model of metachromatic leukodystrophy after intracerebral adeno-associated virus-mediated gene transfer.
Sevin C, Verot L, Benraiss A, Van Dam D, Bonnin D, Nagels G, Fouquet F, Gieselmann V, Vanier MT, De Deyn PP, Aubourg P, Cartier N., Gene Ther 14(5), 2007
PMID: 17093507
Enzyme, cell and gene-based therapies for metachromatic leukodystrophy.
Sevin C, Aubourg P, Cartier N., J Inherit Metab Dis 30(2), 2007
PMID: 17347913
Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum.
Zito E, Buono M, Pepe S, Settembre C, Annunziata I, Surace EM, Dierks T, Monti M, Cozzolino M, Pucci P, Ballabio A, Cosma MP., EMBO J 26(10), 2007
PMID: 17446859
Murine model (Galns(tm(C76S)slu)) of MPS IVA with missense mutation at the active site cysteine conserved among sulfatase proteins.
Tomatsu S, Vogler C, Montaño AM, Gutierrez M, Oikawa H, Dung VC, Orii T, Noguchi A, Sly WS., Mol Genet Metab 91(3), 2007
PMID: 17498992
A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.
Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG., Proc Natl Acad Sci U S A 103(1), 2006
PMID: 16368756
Biomacromolecular interactions, assemblies and machines: a structural view.
Heinz DW, Weiss MS, Wendt KU., Chembiochem 7(1), 2006
PMID: 16317791
Ethanol decreases rat hepatic arylsulfatase A activity levels.
Jean S, Kasinathan C, Buyske S, Manowitz P., Alcohol Clin Exp Res 30(11), 2006
PMID: 17067361
Development of MPS IVA mouse (Galnstm(hC79S.mC76S)slu) tolerant to human N-acetylgalactosamine-6-sulfate sulfatase.
Tomatsu S, Gutierrez M, Nishioka T, Yamada M, Yamada M, Tosaka Y, Grubb JH, Montaño AM, Vieira MB, Trandafirescu GG, Peña OM, Yamaguchi S, Orii KO, Orii T, Noguchi A, Laybauer L., Hum Mol Genet 14(22), 2005
PMID: 16219627

54 References

Daten bereitgestellt von Europe PubMed Central.

The Pfam protein families database.
Bateman A, Birney E, Durbin R, Eddy SR, Howe KL, Sonnhammer EL., Nucleic Acids Res. 28(1), 2000
PMID: 10592242
1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family.
Boltes I, Czapinska H, Kahnert A, von Bulow R, Dierks T, Schmidt B, von Figura K, Kertesz MA, Uson I., Structure 9(6), 2001
PMID: 11435113
Structure of a human lysosomal sulfatase.
Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM., Structure 5(2), 1997
PMID: 9032078
The CCP4 suite: programs for protein crystallography
AUTHOR UNKNOWN, Acta Crystallogr. D50(), 1994
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE., Nat. Struct. Biol. 5(5), 1998
PMID: 9587003
Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation.
Claiborne A, Yeh JI, Mallett TC, Luba J, Crane EJ 3rd, Charrier V, Parsonage D., Biochemistry 38(47), 1999
PMID: 10569923
The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases.
Cosma MP, Pepe S, Annunziata I, Newbold RF, Grompe M, Parenti G, Ballabio A., Cell 113(4), 2003
PMID: 12757706
Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency.
Cosma MP, Pepe S, Parenti G, Settembre C, Annunziata I, Wade-Martins R, Di Domenico C, Di Natale P, Mankad A, Cox B, Uziel G, Mancini GM, Zammarchi E, Donati MA, Kleijer WJ, Filocamo M, Carrozzo R, Carella M, Ballabio A., Hum. Mutat. 23(6), 2004
PMID: 15146462
Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme.
Dickmanns A, Schmidt B, Rudolph MG, Mariappan M, Dierks T, von Figura K, Ficner R., J. Biol. Chem. 280(15), 2005
PMID: 15687489
Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum.
Dierks T, Schmidt B, von Figura K., Proc. Natl. Acad. Sci. U.S.A. 94(22), 1997
PMID: 9342345
Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine.
Dierks T, Miech C, Hummerjohann J, Schmidt B, Kertesz MA, von Figura K., J. Biol. Chem. 273(40), 1998
PMID: 9748219
Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.
Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K., Cell 113(4), 2003
PMID: 12757705
Molecular and biochemical characterisation of a novel sulphatase gene: Arylsulfatase G (ARSG).
Ferrante P, Messali S, Meroni G, Ballabio A., Eur. J. Hum. Genet. 10(12), 2002
PMID: 12461688
Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum.
Fey J, Balleininger M, Borissenko LV, Schmidt B, von Figura K, Dierks T., J. Biol. Chem. 276(50), 2001
PMID: 11600503
Knowledge-based protein secondary structure assignment.
Frishman D, Argos P., Proteins 23(4), 1995
PMID: 8749853
The kinetics of the oxidation of cytochrome c by Paracoccus cytochrome c peroxidase.
Gilmour R, Goodhew CF, Pettigrew GW, Prazeres S, Moura JJ, Moura I., Biochem. J. 300 ( Pt 3)(), 1994
PMID: 8010977
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
Gross E, Sevier CS, Vala A, Kaiser CA, Fass D., Nat. Struct. Biol. 9(1), 2002
PMID: 11740506
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell.
Gross E, Kastner DB, Kaiser CA, Fass D., Cell 117(5), 2004
PMID: 15163408
Calcium-related properties of horseradish peroxidase.
Haschke RH, Friedhoff JM., Biochem. Biophys. Res. Commun. 80(4), 1978
PMID: 416823
Structure of human estrone sulfatase suggests functional roles of membrane association.
Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D., J. Biol. Chem. 278(25), 2003
PMID: 12657638
Protein structure comparison by alignment of distance matrices.
Holm L, Sander C., J. Mol. Biol. 233(1), 1993
PMID: 8377180
Multiple sulfatase deficiency and the nature of the sulfatase family
Hopwood, 2001
Improved methods for building protein models in electron density maps and the location of errors in these models.
Jones TA, Zou JY, Cowan SW, Kjeldgaard M., Acta Crystallogr., A, Found. Crystallogr. 47 ( Pt 2)(), 1991
PMID: 2025413
The extended environment of mononuclear metal centers in protein structures.
Karlin S, Zhu ZY, Karlin KD., Proc. Natl. Acad. Sci. U.S.A. 94(26), 1997
PMID: 9405594
Automated refinement of protein models
Lamzin, Acta Crystallogr. D49(), 1993
PROCHECK: a program to check the stereochemical quality of protein structures.
Laskowski RA, MacArthur MW, Moss DS, Thornton JM., J Appl Crystallogr 26(2), 1993
PMID: c6802
The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.
Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW., Nat. Struct. Biol. 9(5), 2002
PMID: 11938352
A new functional domain of guanine nucleotide dissociation inhibitor (alpha-GDI) involved in Rab recycling.
Luan P, Heine A, Zeng K, Moyer B, Greasely SE, Kuhn P, Balch WE, Wilson IA., Traffic 1(3), 2000
PMID: 11208110
Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis.
Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W., Biochemistry 37(11), 1998
PMID: 9521684
Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme.
Mariappan M, Preusser-Kunze A, Balleininger M, Eiselt N, Schmidt B, Gande SL, Wenzel D, Dierks T, von Figura K., J. Biol. Chem. 280(15), 2005
PMID: 15708861
Satisfying hydrogen bonding potential in proteins.
McDonald IK, Thornton JM., J. Mol. Biol. 238(5), 1994
PMID: 8182748
Raster3D Version 2.0—a program for photorealistic molecular graphics
Merritt, Acta Crystallogr. D50(), 1994
Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine.
Miech C, Dierks T, Selmer T, von Figura K, Schmidt B., J. Biol. Chem. 273(9), 1998
PMID: 9478923
Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans.
Morimoto-Tomita M, Uchimura K, Werb Z, Hemmerich S, Rosen SD., J. Biol. Chem. 277(51), 2002
PMID: 12368295
[20] Processing of X-ray diffraction data collected in oscillation mode.
Otwinowski Z, Minor W., Meth. Enzymol. 276(), 1997
PMID: 27799103
Crystallographic refinement of lignin peroxidase at 2 A.
Poulos TL, Edwards SL, Wariishi H, Gold MH., J. Biol. Chem. 268(6), 1993
PMID: 8440725
Molecular characterization of the human Calpha-formylglycine-generating enzyme.
Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel D, von Figura K, Dierks T., J. Biol. Chem. 280(15), 2005
PMID: 15657036
A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency.
Schmidt B, Selmer T, Ingendoh A, von Figura K., Cell 82(2), 1995
PMID: 7628016
Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution.
Sheriff S, Hendrickson WA, Smith JL., J. Mol. Biol. 197(2), 1987
PMID: 3681996
The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.
Szameit C, Miech C, Balleininger M, Schmidt B, von Figura K, Dierks T., J. Biol. Chem. 274(22), 1999
PMID: 10336424
Biochemical basis of oxidative protein folding in the endoplasmic reticulum.
Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS., Science 290(5496), 2000
PMID: 11090354
Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes.
Vranka JA, Sakai LY, Bachinger HP., J. Biol. Chem. 279(22), 2004
PMID: 15044469

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