Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae

Journal of Molecular Biology

Volumn 268, Issue 1, 1997, Pages 137-146

  Hu, Shu Hong ^a   Peek, Joel A ^b   Rattigan, Eileen ^c   Taylor, Ronald K ^d   Martin, Jennifer L ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b Lederle Praxis Biologicals ^*  (United States)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

DsbA; Oxidoreductase; Protein structure; Thioredoxin fold; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; CHOLERA TOXIN; OXIDOREDUCTASE; OXIDOREDUCTASE INHIBITOR; PROLINE; THIOREDOXIN; VIRULENCE FACTOR;

ARTICLE; BACTERIAL COLONIZATION; BACTERIAL VIRULENCE; BACTERIUM PILUS; CRYSTAL STRUCTURE; DISULFIDE BOND; DRUG DESIGN; ENZYME ACTIVE SITE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; VIBRIO CHOLERAE;

EID: 0031585999     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0940     Document Type: Article

References (48)

1. Bacon D. J., Anderson W. F. A fast algorithm for rendering space filling molecular pictures. J. Mol. Graphics. 6:1988;219-222.
2. Bardwell J. C. A., McGovern K., Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell. 67:1991;581-589.
3. Bhat T. N., Cohen G. H. OMITMAP: an electron density map suitable for the examination of errors in a macromolecular model. J. Appl. Crystallog. 17:1984;244-248.
4. Brünger A. T. Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Crystallog. sect. A. 46:1990;46-57.
5. Brünger A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992a;472-475.
6. Brünger A. T. X-PLOR (Version 3.1) Manual. 1992b;Yale University, New Haven.
7. Brünger A. T. Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallog. sect. D. 49:1993;24-36.
8. Dyson H. J., Gippert G. P., Case D. A., Holmgren A., Wright P. E. Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magentic resonance spectroscopy. Biochemistry. 29:1990;4129-4136.
9. Eklund H., Gleason F. S., Holmgren A. Structural and functional relations among thioredoxins of different species. Proteins: Struct. Funct. Genet. 11:1991;13-28.
10. Eklund H., Ingelman M., Söderberg B.-O., Uhlin T., Nordlund P., Nikkola M., Sonnerstam U., Joelsson T., Petratos K. Structure of oxidized bacteriophage T4 glutaredoxin (thioredoxin) refinement of native and mutant proteins. J. Mol. Biol. 228:1992;596-618.
11. Engh R. A., Huber R. Accurate bond lengths and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect A. 47:1991;392-400.
12. Forman-Kay J. D., Clore G. M., Wingfield P. T., Gronenborn A. M. High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry. 30:1991;2685-2698.
13. Grauschopf U., Winther J., Korber P., Zander T., Dallinger P., Bardwell J. C. A. Why is DsbA such an oxidizing disulfide catalyst? Cell. 83:1995;947-955.
14. Guddat L. W., Bardwell J. C. A., Zander T., Martin J. L. The uncharged surface features surrounding the active-site of E. coli DsbA are conserved and are implicated in peptide binding. Protein Sci. 1997.
15. Hennecke J., Spleiss C., Glockshuber R. Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA. J. Biol. Chem. 272 (1):1997;189-195.
16. Herron J. N., He X. M., Ballard D. W., Blier P. R., Pace P. E., Bothwell A. L. M., Voss E. W., Jr, Edmundson A. B. An autoantibody to single-stranded DNA: comparison of the three-dimensional structures of the unliganded Fab and a deoxynucleotide-Fab complex. Proteins: Struct. Funct. Genet. 11:1991;159-175.
17. Huber R., Epp O., Steigemann W., Formanek H. The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin. Eur. J. Biochem. 19:1971;42-50.
18. Hutchinson E. G., Thornton J. M. PROMOTIF: a program to identify and analyze structural motifs in proteins. Protein Sci. 5:1996;212-220.
19. 13C NMR. Biochemistry. 35 (1):1996;1-6.
20. Jeng M.-F., Campbell A. P., Begley T., Holmgren A., Case D. A., Wright P. E., Dyson H. J. High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure. 2:1994;853-868.
21. Jeng M.-F., Holmgren A., Dyson H. J. Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction. Biochemistry. 34 (32):1995;10101-10105.
22. Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
23. Katti S. K., LeMaster D. M., Eklund H. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J. Mol. Biol. 212:1990;167-184.
24. 15N NMR spectroscopy. Biochemistry. 35:1996;7684-7691.
25. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
26. Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
27. Luzzati V. Traitment statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810.
28. Martin J. L. Thioredoxin: a fold for all reasons. Structure. 3 (3):1995;245-250.
29. Martin J. L., Bardwell J. C. A., Kuriyan J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature. 365:1993a;464-468.
30. Martin J. L., Waksman G., Bardwell J. C. A., Beckwith J., Kuriyan J. Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J. Mol. Biol. 230:1993b;1097-1100.
31. Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
32. McGregor M. J., Islam S. A., Sternberg M. J. E. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J. Mol. Biol. 198:1987;295-310.
33. Merritt E. A., Murphy M. E. P. Raster3D Version 2.0. A Program for Photorealistic Molecular Graphics. Acta Crystallog. sect. D. 50:1994;869-873.
34. Nicholls A., Bharadwaj R., Honig B. GRASP: graphical representation and analysis of surface properties. Biophys. J. 64:1993;A116.
35. Peek J. A., Taylor R. K. Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae. Proc. Natl Acad. Sci. USA. 89:1992;6210-6214.
36. Peterson K. M., Mekalanos J. J. Characterization of the Vibrio cholerae regulon: identification of novel genes involved in intestinal colonization. Infect. Immun. 56:1988;2822-2829.
37. Qin J., Clore G. M., Gronenborn A. M. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure. 2:1994;503-522.
38. Qin J., Clore G. M., Gronenborn A. M. Ionization equilibria for side-chain carboxyl groups in oxidized and reduced human thioredoxin and in the complex with its target peptide from the transcription factor NFκB. Biochemistry. 35:1996;7-13.
39. Shevchik V. E., Bortoli-German I., Robert-Baudouy J., Robinet S., Barras F., Condemine G. Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi. Mol. Microbiol. 16 (4):1995;745-753.
40. Sun D., Lafferty M. J., Peek J. A., Taylor R. K. Domains within the Vibrio cholerae toxin coregulated pilin subunit that mediate bacterial colonization. Gene. in the press:1997.
41. Tomb J.-F. A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd. Proc. Natl Acad. Sci., USA. 89:1992;10252-10256.
42. Watarai M., Tobe T., Yoshikawa M., Sasakawa C. Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells. Proc. Natl Acad. Sci. USA. 92 (11):1995;4927-4931.
43. Weichsel A., Gasdaska J. R., Powis G., Montfort W. R. Crystal structure of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure. 4:1996;735-751.
44. Wilson A. J. C. The probability distribution of X-ray intensities. Acta Crystallog. 2:1949;318-321.
45. a>9. Biochemistry. 34:1995;8931-8939.
46. Yu J., Webb H., Hurst T. R. A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for the enterotoxin biogenesis in Vibrio cholerae. Mol. Microbiol. 6:1992;1949-1958.
47. Yu J., McLaughlin S., Freedman R. B., Hirst T. R. Cloning and active site mutagenesis of Vibrio cholerae DsbA, a periplasmic enzyme that catalyzes disulfide bond formation. J. Biol. Chem. 268:1993;4326-4330.
48. Zhang H.-Z., Donnenberg M. S. DsbA is required for stability of the type IV pilin of enteropathogenic Escherichia coli. Mol. Microbiol. 21 (4):1996;787-797.