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 (2006)
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 103(1): 81-86.
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Autor*in
Roeser, D;
Preusser-Kunze, A;
Schmidt, B;
Gasow, K;
Wittmann, JG;
Dierks, ThomasUniBi;
von Figura, K;
Rudolph, MG
Einrichtung
Abstract / Bemerkung
The formylglycine (FGly)-generating enzyme (FGE) uses molecular oxygen to oxidize a conserved cysteine residue in all eukaryotic sulfatases to the catalytically active FGly. Sulfatases degrade and remodel sulfate esters, and inactivity of FGE results in multiple sulfatase deficiency, a fatal disease. The previously determined FGE crystal structure revealed two crucial cysteine residues in the active site, one of which was thought to be implicated in substrate binding. The other cysteine residue partakes in a novel oxygenase mechanism that does not rely on any cofactors. Here, we present crystal structures of the individual FGE cysteine mutants and employ chemical probing of wild-type FGE, which defined the cysteines to differ strongly in their reactivity. This striking difference in reactivity is explained by the distinct roles of these cysteine residues in the catalytic mechanism. Hitherto, an enzyme-substrate complex as an essential cornerstone for the structural evaluation of the FGly formation mechanism has remained elusive. We also present two FGE-substrate complexes with pentamer and heptamer peptides that mimic sulfatases. The peptides isolate a small cavity that is a likely binding site for molecular oxygen and could host reactive oxygen intermediates during cysteine oxidation. Importantly, these FGE-peptide complexes directly unveil the molecular bases of FGE substrate binding and specificity. Because of the conserved nature of FGE sequences in other organisms, this binding mechanism is of general validity. Furthermore, several disease-causing mutations in both FGE and sulfatases are explained by this binding mechanism.
Stichworte
enzyme mechanism;
posttranslational modification;
oxygenase
Erscheinungsjahr
2006
Zeitschriftentitel
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Band
103
Ausgabe
1
Seite(n)
81-86
ISSN
0027-8424
eISSN
1091-6490
Page URI
https://pub.uni-bielefeld.de/record/1600859
Zitieren
Roeser D, Preusser-Kunze A, Schmidt B, et al. A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2006;103(1):81-86.
Roeser, D., Preusser-Kunze, A., Schmidt, B., Gasow, K., Wittmann, J. G., Dierks, T., von Figura, K., et al. (2006). A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 103(1), 81-86. https://doi.org/10.1073/pnas.0507592102
Roeser, D, Preusser-Kunze, A, Schmidt, B, Gasow, K, Wittmann, JG, Dierks, Thomas, von Figura, K, and Rudolph, MG. 2006. “A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme”. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 103 (1): 81-86.
Roeser, D., Preusser-Kunze, A., Schmidt, B., Gasow, K., Wittmann, J. G., Dierks, T., von Figura, K., and Rudolph, M. G. (2006). A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 103, 81-86.
Roeser, D., et al., 2006. A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 103(1), p 81-86.
D. Roeser, et al., “A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme”, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 103, 2006, pp. 81-86.
Roeser, D., Preusser-Kunze, A., Schmidt, B., Gasow, K., Wittmann, J.G., Dierks, T., von Figura, K., Rudolph, M.G.: A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 103, 81-86 (2006).
Roeser, D, Preusser-Kunze, A, Schmidt, B, Gasow, K, Wittmann, JG, Dierks, Thomas, von Figura, K, and Rudolph, MG. “A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme”. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 103.1 (2006): 81-86.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
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UNIPROT
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PDB
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x-ray diffraction (PDB: 2aij)
Protein structure name: formylglycine generating enzyme c336s mutant covalently bound to substrate peptide ctpsr
Public wwPDB file in PDB format
Protein structure name: formylglycine generating enzyme c336s mutant covalently bound to substrate peptide ctpsr
Public wwPDB file in PDB format
x-ray diffraction (PDB: 2aii)
Protein structure name: wild-type formylglycine generating enzyme reacted with iodoacetamide
Public wwPDB file in PDB format
Protein structure name: wild-type formylglycine generating enzyme reacted with iodoacetamide
Public wwPDB file in PDB format
x-ray diffraction (PDB: 2afy)
Protein structure name: formylglycine generating enzyme c341s mutant
Public wwPDB file in PDB format
Protein structure name: formylglycine generating enzyme c341s mutant
Public wwPDB file in PDB format
x-ray diffraction (PDB: 2aft)
Protein structure name: formylglycine generating enzyme c336s mutant
Public wwPDB file in PDB format
Protein structure name: formylglycine generating enzyme c336s mutant
Public wwPDB file in PDB format
x-ray diffraction (PDB: 2aik)
Protein structure name: formylglycine generating enzyme c336s mutant covalently bound to substrate peptide lctpsra
Public wwPDB file in PDB format
Protein structure name: formylglycine generating enzyme c336s mutant covalently bound to substrate peptide lctpsra
Public wwPDB file in PDB format
OMIM
1 Eintrag gefunden, die diesen Artikel zitieren
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Roeser D, Dickmanns A, Gasow K, Rudolph MG., Acta Crystallogr. D Biol. Crystallogr. 61(Pt 8), 2005
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Roeser D, Dickmanns A, Gasow K, Rudolph MG., Acta Crystallogr. D Biol. Crystallogr. 61(Pt 8), 2005
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The CCP4 suite: programs for protein crystallography.
Collaborative Computational Project, Number 4., Acta Crystallogr. D Biol. Crystallogr. 50(Pt 5), 1994
PMID: 15299374
Collaborative Computational Project, Number 4., Acta Crystallogr. D Biol. Crystallogr. 50(Pt 5), 1994
PMID: 15299374
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures.
Brunger AT., Nature 355(6359), 1992
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Satisfying hydrogen bonding potential in proteins.
McDonald IK, Thornton JM., J. Mol. Biol. 238(5), 1994
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McDonald IK, Thornton JM., J. Mol. Biol. 238(5), 1994
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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
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Sheriff S, Hendrickson WA, Smith JL., J. Mol. Biol. 197(2), 1987
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Electrostatics of nanosystems: application to microtubules and the ribosome.
Baker NA, Sept D, Joseph S, Holst MJ, McCammon JA., Proc. Natl. Acad. Sci. U.S.A. 98(18), 2001
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Raster3D Version 2.0. A program for photorealistic molecular graphics.
Merritt EA, Murphy ME., Acta Crystallogr. D Biol. Crystallogr. 50(Pt 6), 1994
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Merritt EA, Murphy ME., Acta Crystallogr. D Biol. Crystallogr. 50(Pt 6), 1994
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The atomic structure of protein-protein recognition sites.
Lo Conte L, Chothia C, Janin J., J. Mol. Biol. 285(5), 1999
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Crystal structures of two rat MHC class Ia (RT1-A) molecules that are associated differentially with peptide transporter alleles TAP-A and TAP-B.
Rudolph MG, Stevens J, Speir JA, Trowsdale J, Butcher GW, Joly E, Wilson IA., J. Mol. Biol. 324(5), 2002
PMID: 12470953
Rudolph MG, Stevens J, Speir JA, Trowsdale J, Butcher GW, Joly E, Wilson IA., J. Mol. Biol. 324(5), 2002
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Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase.
Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K., Mol. Cell 11(2), 2003
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Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K., Mol. Cell 11(2), 2003
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Shape complementarity at protein/protein interfaces.
Lawrence MC, Colman PM., J. Mol. Biol. 234(4), 1993
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Lawrence MC, Colman PM., J. Mol. Biol. 234(4), 1993
PMID: 8263940
Antibody catalysis of the oxidation of water.
Wentworth P Jr, Jones LH, Wentworth AD, Zhu X, Larsen NA, Wilson IA, Xu X, Goddard WA 3rd, Janda KD, Eschenmoser A, Lerner RA., Science 293(5536), 2001
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Oxygenases without requirement for cofactors or metal ions.
Fetzner S., Appl. Microbiol. Biotechnol. 60(3), 2002
PMID: 12436305
Fetzner S., Appl. Microbiol. Biotechnol. 60(3), 2002
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Structural and thermodynamic correlates of T cell signaling.
Rudolph MG, Luz JG, Wilson IA., Annu Rev Biophys Biomol Struct 31(), 2001
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Rudolph MG, Luz JG, Wilson IA., Annu Rev Biophys Biomol Struct 31(), 2001
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Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases.
Dierks T, Lecca MR, Schlotterhose P, Schmidt B, von Figura K., EMBO J. 18(8), 1999
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Dierks T, Lecca MR, Schlotterhose P, Schmidt B, von Figura K., EMBO J. 18(8), 1999
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Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS-VI patients.
Litjens T, Brooks DA, Peters C, Gibson GJ, Hopwood JJ., Am. J. Hum. Genet. 58(6), 1996
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Litjens T, Brooks DA, Peters C, Gibson GJ, Hopwood JJ., Am. J. Hum. Genet. 58(6), 1996
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Molecular basis of iduronate-2-sulphatase gene mutations in patients with mucopolysaccharidosis type II (Hunter syndrome).
Li P, Bellows AB, Thompson JN., J. Med. Genet. 36(1), 1999
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Li P, Bellows AB, Thompson JN., J. Med. Genet. 36(1), 1999
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Detection of four novel mutations in the iduronate-2-sulfatase gene. Mutations in brief no. 123. Online.
Balzano N, Villani GR, Grosso M, Izzo P, Di Natale P., Hum. Mutat. 11(4), 1998
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Balzano N, Villani GR, Grosso M, Izzo P, Di Natale P., Hum. Mutat. 11(4), 1998
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Molecular basis of mucopolysaccharidosis type II: mutations in the iduronate-2-sulphatase gene.
Hopwood JJ, Bunge S, Morris CP, Wilson PJ, Steglich C, Beck M, Schwinger E, Gal A., Hum. Mutat. 2(6), 1993
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Hopwood JJ, Bunge S, Morris CP, Wilson PJ, Steglich C, Beck M, Schwinger E, Gal A., Hum. Mutat. 2(6), 1993
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Iduronate-2-sulfatase gene mutations in 16 patients with mucopolysaccharidosis type II (Hunter syndrome).
Bunge S, Steglich C, Zuther C, Beck M, Morris CP, Schwinger E, Schinzel A, Hopwood JJ, Gal A., Hum. Mol. Genet. 2(11), 1993
PMID: 8281149
Bunge S, Steglich C, Zuther C, Beck M, Morris CP, Schwinger E, Schinzel A, Hopwood JJ, Gal A., Hum. Mol. Genet. 2(11), 1993
PMID: 8281149
Identification of 16 sulfamidase gene mutations including the common R74C in patients with mucopolysaccharidosis type IIIA (Sanfilippo A).
Bunge S, Ince H, Steglich C, Kleijer WJ, Beck M, Zaremba J, van Diggelen OP, Weber B, Hopwood JJ, Gal A., Hum. Mutat. 10(6), 1997
PMID: 9401012
Bunge S, Ince H, Steglich C, Kleijer WJ, Beck M, Zaremba J, van Diggelen OP, Weber B, Hopwood JJ, Gal A., Hum. Mutat. 10(6), 1997
PMID: 9401012
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
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
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
Dickmanns A, Schmidt B, Rudolph MG, Mariappan M, Dierks T, von Figura K, Ficner R., J. Biol. Chem. 280(15), 2005
PMID: 15687489
Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2.
Zito E, Fraldi A, Pepe S, Annunziata I, Kobinger G, Di Natale P, Ballabio A, Cosma MP., EMBO Rep. 6(7), 2005
PMID: 15962010
Zito E, Fraldi A, Pepe S, Annunziata I, Kobinger G, Di Natale P, Ballabio A, Cosma MP., EMBO Rep. 6(7), 2005
PMID: 15962010
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
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
Mutations of the iduronate-2-sulfatase gene in 12 Polish patients with mucopolysaccharidosis type II (Hunter syndrome).
Popowska E, Rathmann M, Tylki-Szymanska A, Bunge S, Steglich C, Schwinger E, Gal A., Hum. Mutat. 5(1), 1995
PMID: 7728156
Popowska E, Rathmann M, Tylki-Szymanska A, Bunge S, Steglich C, Schwinger E, Gal A., Hum. Mutat. 5(1), 1995
PMID: 7728156
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