Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI

Niemann H, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW (2006)
J Mol Biol 356(1): 1-8.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
DOI
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ;
Einrichtung
Fakultät für Chemie > Biochemie IV
Stichworte
Crystallography; X-Ray; Disulfides/*chemistry/metabolism; Tertiary; Histidine/genetics/metabolism; Momordica/*chemistry/genetics; Molecular Sequence Data; Molecular; Models; Nuclear Magnetic Resonance; Biomolecular; Plant Proteins/*chemistry/genetics/*metabolism; Protein Structure; Recombinant Fusion Proteins/chemistry/genetics/metabolism; Ribonucleases/genetics/*metabolism; Sequence Alignment; Amino Acid Sequence
Erscheinungsjahr
2006
Zeitschriftentitel
J Mol Biol
Band
356
Zeitschriftennummer
1
Seite
1-8
ISSN
0022-2836
PUB-ID

Zitieren

Niemann H, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW. Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol. 2006;356(1):1-8.
Niemann, H., Schmoldt, H. U., Wentzel, A., Kolmar, H., & Heinz, D. W. (2006). Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol, 356(1), 1-8. doi:10.1016/j.jmb.2005.11.005
Niemann, H., Schmoldt, H. U., Wentzel, A., Kolmar, H., and Heinz, D. W. (2006). Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol 356, 1-8.
Niemann, H., et al., 2006. Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol, 356(1), p 1-8.
H. Niemann, et al., “Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI”, J Mol Biol, vol. 356, 2006, pp. 1-8.
Niemann, H., Schmoldt, H.U., Wentzel, A., Kolmar, H., Heinz, D.W.: Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol. 356, 1-8 (2006).
Niemann, Hartmut, Schmoldt, H. U., Wentzel, A., Kolmar, H., and Heinz, D. W. “Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI”. J Mol Biol 356.1 (2006): 1-8.

10 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

T4 lysozyme-facilitated crystallization of the human molybdenum cofactor-dependent enzyme mARC.
Kubitza C, Ginsel C, Bittner F, Havemeyer A, Clement B, Scheidig AJ., Acta Crystallogr F Struct Biol Commun 74(pt 6), 2018
PMID: 29870017
Cellular disulfide bond formation in bioactive peptides and proteins.
Patil NA, Tailhades J, Hughes RA, Separovic F, Wade JD, Hossain MA., Int J Mol Sci 16(1), 2015
PMID: 25594871
PredSTP: a highly accurate SVM based model to predict sequential cystine stabilized peptides.
Islam SM, Sajed T, Kearney CM, Baker EJ., BMC Bioinformatics 16(), 2015
PMID: 26142484
Barnase and binase: twins with distinct fates.
Ulyanova V, Vershinina V, Ilinskaya O., FEBS J 278(19), 2011
PMID: 21824291
Engineered cystine knot miniproteins as potent inhibitors of human mast cell tryptase beta.
Sommerhoff CP, Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Diederichsen U, Kolmar H., J Mol Biol 395(1), 2010
PMID: 19852971
Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.
de Marco A., Microb Cell Fact 8(), 2009
PMID: 19442264
Head-to-tail cyclized cystine-knot peptides by a combined recombinant and chemical route of synthesis.
Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Wentzel A, Frauendorf H, Sommerhoff CP, Diederichsen U, Kolmar H., Chembiochem 9(1), 2008
PMID: 18058774
Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides.
Thongyoo P, Roqué-Rosell N, Leatherbarrow RJ, Tate EW., Org Biomol Chem 6(8), 2008
PMID: 18385853
Evaluation and improvement of the properties of the novel cystine-knot microprotein McoEeTI for oral administration.
Werle M, Kafedjiiski K, Kolmar H, Bernkop-Schnürch A., Int J Pharm 332(1-2), 2007
PMID: 17070661
Eukaryotic integral membrane protein expression utilizing the Escherichia coli glycerol-conducting channel protein (GlpF).
Neophytou I, Harvey R, Lawrence J, Marsh P, Panaretou B, Barlow D., Appl Microbiol Biotechnol 77(2), 2007
PMID: 17828601

42 References

Daten bereitgestellt von Europe PubMed Central.

The cystine knot motif in toxins and implications for drug design.
Craik DJ, Daly NL, Waine C., Toxicon 39(1), 2001
PMID: 10936622
Structure of a hybrid squash inhibitor in complex with porcine pancreatic elastase at 1.8 A resolution.
Ay J, Hilpert K, Krauss N, Schneider-Mergener J, Hohne W., Acta Crystallogr. D Biol. Crystallogr. 59(Pt 2), 2003
PMID: 12554935
The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides.
Christmann A, Walter K, Wentzel A, Kratzner R, Kolmar H., Protein Eng. 12(9), 1999
PMID: 10506290
Cystine knots.
Isaacs NW., Curr. Opin. Struct. Biol. 5(3), 1995
PMID: 7583638
A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides.
Pallaghy PK, Nielsen KJ, Craik DJ, Norton RS., Protein Sci. 3(10), 1994
PMID: 7849598
A fusion protein system for the recombinant production of short disulfide bond rich cystine knot peptides using barnase as a purification handle.
Schmoldt HU, Wentzel A, Becker S, Kolmar H., Protein Expr. Purif. 39(1), 2005
PMID: 15596363
Expression of Bacillus amyloliquefaciens extracellular ribonuclease (barnase) in Escherichia coli following an inactivating mutation.
Paddon CJ, Hartley RW., Gene 53(1), 1987
PMID: 3297926
In vivo system for the detection of low level activity barnase mutants.
Jucovic M, Hartley RW., Protein Eng. 8(5), 1995
PMID: 8532672
Solution structure of the squash trypsin inhibitor MCoTI-II. A new family for cyclic knottins.
Heitz A, Hernandez JF, Gagnon J, Hong TT, Pham TT, Nguyen TM, Le-Nguyen D, Chiche L., Biochemistry 40(27), 2001
PMID: 11434766
Circular proteins in plants: solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis.
Felizmenio-Quimio ME, Daly NL, Craik DJ., J. Biol. Chem. 276(25), 2001
PMID: 11292835
Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure.
Hernandez JF, Gagnon J, Chiche L, Nguyen TM, Andrieu JP, Heitz A, Trinh Hong T, Pham TT, Le Nguyen D., Biochemistry 39(19), 2000
PMID: 10801322
Protease inhibitors from Ecballium elaterium seeds.
Favel A, Mattras H, Coletti-Previero MA, Zwilling R, Robinson EA, Castro B., Int. J. Pept. Protein Res. 33(3), 1989
PMID: 2654042
Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme.
Hayward S, Berendsen HJ., Proteins 30(2), 1998
PMID: 9489922
Molecular structure of a new family of ribonucleases.
Mauguen Y, Hartley RW, Dodson EJ, Dodson GG, Bricogne G, Chothia C, Jack A., Nature 297(5862), 1982
PMID: 7078632
Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution.
Buckle AM, Fersht AR., Biochemistry 33(7), 1994
PMID: 8110767
Crystal structure of a barnase-d(GpC) complex at 1.9 A resolution.
Baudet S, Janin J., J. Mol. Biol. 219(1), 1991
PMID: 2023257
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features.
Kabsch W, Sander C., Biopolymers 22(12), 1983
PMID: 6667333
The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes.
Bode W, Greyling HJ, Huber R, Otlewski J, Wilusz T., FEBS Lett. 242(2), 1989
PMID: 2914611
Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination.
Thaimattam R, Tykarska E, Bierzynski A, Sheldrick GM, Jaskolski M., Acta Crystallogr. D Biol. Crystallogr. 58(Pt 9), 2002
PMID: 12198301
High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
Helland R, Berglund GI, Otlewski J, Apostoluk W, Andersen OA, Willassen NP, Smalas AO., Acta Crystallogr. D Biol. Crystallogr. 55(Pt 1), 1999
PMID: 10089404
Use of restrained molecular dynamics in water to determine three-dimensional protein structure: prediction of the three-dimensional structure of Ecballium elaterium trypsin inhibitor II.
Chiche L, Gaboriaud C, Heitz A, Mornon JP, Castro B, Kollman PA., Proteins 6(4), 1989
PMID: 2622910
An 1H NMR determination of the three-dimensional structures of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium elaterium (EETI-II).
Nielsen KJ, Alewood D, Andrews J, Kent SB, Craik DJ., Protein Sci. 3(2), 1994
PMID: 8003965
Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): a rigid molecular scaffold.
Kratzner R, Debreczeni JE, Pape T, Schneider TR, Wentzel A, Kolmar H, Sheldrick GM, Uson I., Acta Crystallogr. D Biol. Crystallogr. 61(Pt 9), 2005
PMID: 16131759
Beta-and gamma-turns in proteins revisited: a new set of amino acid turn-type dependent positional preferences and potentials.
Guruprasad K, Rajkumar S., J. Biosci. 25(2), 2000
PMID: 10878855
Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems.
Terpe K., Appl. Microbiol. Biotechnol. 60(5), 2002
PMID: 12536251
Structural analysis of regulatory protein domains using GST-fusion proteins.
Zhan Y, Song X, Zhou GW., Gene 281(1-2), 2001
PMID: 11750122
Crystal structures of fusion proteins with large-affinity tags.
Smyth DR, Mrozkiewicz MK, McGrath WJ, Listwan P, Kobe B., Protein Sci. 12(7), 2003
PMID: 12824478
Crystal structure of a dominant B-cell epitope from the preS2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein.
Saul FA, Vulliez-le Normand B, Lema F, Bentley GA., J. Mol. Biol. 280(2), 1998
PMID: 9654443
Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins.
Kobe B, Center RJ, Kemp BE, Poumbourios P., Proc. Natl. Acad. Sci. U.S.A. 96(8), 1999
PMID: 10200260
Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera.
Ke A, Wolberger C., Protein Sci. 12(2), 2003
PMID: 12538894
Crystal structure of the SarR protein from Staphylococcus aureus.
Liu Y, Manna A, Li R, Martin WE, Murphy RC, Cheung AL, Zhang G., Proc. Natl. Acad. Sci. U.S.A. 98(12), 2001
PMID: 11381122
Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside.
Kukimoto M, Nureki O, Shirouzu M, Katada T, Hirabayashi Y, Sugiya H, Furuyama S, Yokoyama S, Hara-Yokoyama M., J. Biochem. 127(2), 2000
PMID: 10731682
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.
Adikesavan NV, Mahmood SS, Stanley N, Xu Z, Wu N, Thibonnier M, Shoham M., Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61(Pt 4), 2005
PMID: 16511036
Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.
Niemann HH, Knetsch ML, Scherer A, Manstein DJ, Kull FJ., EMBO J. 20(21), 2001
PMID: 11689422
The KNOTTIN website and database: a new information system dedicated to the knottin scaffold.
Gelly JC, Gracy J, Kaas Q, Le-Nguyen D, Heitz A, Chiche L., Nucleic Acids Res. 32(Database issue), 2004
PMID: 14681383
Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
Kabsch, J. Appl. Crystallog. 26(), 1993
Rapid automated molecular replacement by evolutionary search.
Kissinger CR, Gehlhaar DK, Fogel DB., Acta Crystallogr. D Biol. Crystallogr. 55(Pt 2), 1999
PMID: 10089360
Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals.
Kantardjieff KA, Rupp B., Protein Sci. 12(9), 2003
PMID: 12930986
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
Macromolecular TLS refinement in REFMAC at moderate resolutions.
Winn MD, Murshudov GN, Papiz MZ., Meth. Enzymol. 374(), 2003
PMID: 14696379
ARP/wARP and molecular replacement.
Perrakis A, Harkiolaki M, Wilson KS, Lamzin VS., Acta Crystallogr. D Biol. Crystallogr. 57(Pt 10), 2001
PMID: 11567158
Improved R-factors for diffraction data analysis in macromolecular crystallography.
Diederichs K, Karplus PA., Nat. Struct. Biol. 4(4), 1997
PMID: 9095194

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 16337652
PubMed | Europe PMC

Suchen in

Google Scholar