Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell

Cell

Volumn 117, Issue 5, 2004, Pages 601-610

  Gross, Einav ^a   Kastner, David B ^a   Kaiser, Chris A ^b   Fass, Deborah ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE DERIVATIVE; FLAVOPROTEIN; PROTEIN ERO1P; PROTEIN ERV2P; THIOL OXIDASE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; DISULFIDE BOND; OXIDATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

EID: 2542475140     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(04)00418-0     Document Type: Article

References (48)

1. Bader M., Muse W., Ballou D.P., Gassner C., Bardwell J.C. Oxidative protein folding is driven by the electron transport system. Cell. 98:1999;217-227
2. Becher D., Kricke J., Stein G., Lisowsky T. A mutant for the yeast scERV1 gene displays a new defect in mitochondrial morphology and distribution. Yeast. 15:1999;1171-1181
3. Benham A.M., Cabibbo A., Fassio A., Bulleid N., Sitia R., Braakman I. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha. EMBO J. 19:2000;4493-4502
4. Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., Bulleid N.J., Sitia R. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275:2000;4827-4833
5. Carson M. Ribbons. Methods Enzymol. 277:1997;493-505
6. Collet F.J., Bardwell J.C.A. Oxidative protein folding in bacteria. Mol. Microbiol. 44:2002;1-8
7. Coppock D.L., Cina-Poppe D., Gilleran S. The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families. thioredoxin and ERV1 Genomics. 54:1998;460-468
8. Cuozzo J.W., Kaiser C.A. Competition between glutathione and protein thiols for disulphide-bond formation. Nat. Cell Biol. 1:1999;130-135
9. De La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494
10. Dym O., Eisenberg D. Sequence-structure analysis of FAD-containing proteins. Protein Sci. 10:2001;1712-1728
11. Frand A.R., Kaiser C.A. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell. 1:1998;161-170
12. Frand A.R., Kaiser C.A. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell. 4:1999;469-477
13. Frand A.R., Kaiser C.A. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol. Biol. Cell. 11:2000;2833-2843
14. Gerber J., Muhlenhoff U., Hofhaus G., Lill R., Lisowsky T. Yeast Erv2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family. J. Biol. Chem. 276:2001;22486-22491
15. Gibrat J.-F., Madej T., Bryant S.H. Surprising similarities in structure comparison. Curr. Opin. Struct. Biol. 6:1996;377-385
16. Grauschopf U., Fritz A., Glockshuber R. Mechanism of the electron transfer catalyst DsbB from Escherichia coli. EMBO J. 22:2003;3503-3513
17. Gross E., Sevier C., Vala A., Kaiser C.A., Fass D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9:2002;61-67
18. Hofhaus G., Lee J.-E., Tews I., Rosenberg B., Lisowsky T. The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vitro activity and interacts with the primary redox center. Eur. J. Biochem. 270:2003;1528-1535
19. Holm L., Sander C. Dictionary of recurrent domains in protein structures. Proteins. 33:1998;88-96
20. Hoober K.L., Thorpe C. Egg white sulfhydryl oxidase. kinetic mechanism of the catalysis of disulfide bond formation Biochemistry. 38:1999;3211-3217
21. Hoober K.L., Joneja B., White H.B. III, Thorpe C. A sulfhydryl oxidase from chicken egg white. J. Biol. Chem. 271:1996;30510-30516
22. Hoober K.L., Glynn N.M., Burnside J., Coppock D.L., Thorpe C. Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases. J. Biol. Chem. 274:1999;31759-31762
23. 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 Crystallogr. A. 47:1991;110-119
24. Jung Y.S., Bonagura C.A., Tilley G.J., Gao-Sheridan H.S., Armstrong F.A., Stout C.D., Burgess B.K. Structure of C42D Azotobacter vinelandii FdI. A Cys-X-X-Asp-X-X-Cys motif ligates an air-stable [4Fe-4S]2+/+ cluster. J. Biol. Chem. 275:2000;36974-36983
25. Kadokura H., Beckwith J. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J. 21:2002;2354-2363
26. Kobayashi T., Ito K. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. EMBO J. 18:1999;1192-1198
27. Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950
28. Lario P.I., Sampson N., Vrielink A. Sub-atomic resolution crystal structure of cholesterol oxidase. what atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity J. Mol. Biol. 326:2003;1635-1650
29. Lee B., Richards F.M. The interpretation of protein structures. estimation of static accessibility J. Mol. Biol. 55:1971;379-400
30. Linke K., Jakob U. Not every disulfide lasts forever. disulfide bond formation as a redox switch Antioxid. Redox Signal. 5:2003;425-434
31. Niimura Y., Nishiyama Y., Saito D., Tsuji H., Hidaka M., Miyaji T., Watanabe T., Massey V. A hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase in Amphibacillus xylanus. J. Bacteriol. 182:2000;5046-5051
32. Noiva R. Protein disulfide isomerase. the multifunctional redox chaperone of the endoplasmic reticulum Semin. Cell Dev. Biol. 10:1999;481-493
33. Notredame C., Higgins D., Heringa J. T-Coffee. A novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302:2000;205-217
34. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
35. Pace C.N., Grimsley G.R., Thomson J.A., Barnett B.J. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem. 263:1988;11820-11825
36. Pollard G.M., Travers J.K., Weissman J.S. Ero1p. A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum Mol. Cell. 1:1998;171-182
37. Raje S., Thorpe C. A continuous fluorescence assay for sulfhydryl oxidase. Anal. Biochem. 307:2002;266-272
38. Raje S., Thorpe C. Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family. role of a thioredoxin domain in disulfide bond formation Biochemistry. 42:2003;4560-4568
39. Regeimbal J., Gleiter S., Trumpower B.L., Yu C.A., Diwakar M., Ballou D.P., Bardwell J.C. Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc. Natl. Acad. Sci. USA. 100:2003;13779-13784
40. Salamov A.A., Solovyev V.V. Prediction of protein secondary structure by combinin nearest-neighbr algorithms and multiple sequence alignment. J. Mol. Biol. 247:1995;11-15
41. Senkevich T.G., White C.L., Koonin E.V., Moss B. A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation. Proc. Natl. Acad. Sci. USA. 97:2000;12068-12073
42. Sevier C.S., Kaiser C.A. Formation and transfer of disulphide bonds in living cells. Nat. Rev. Mol. Cell Biol. 3:2002;836-847
43. Sevier C.S., Cuozzo J.W., Vala A., Aslund F., Kaiser C.A. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat. Cell Biol. 3:2001;874-882
44. Terwilliger T., Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. D. Biol. Crystallogr. 55:1999;849-861
45. Tu B.P., Weissman J.S. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell. 10:2002;983-994
46. Tu B.P., Weissman J.S. Oxidative protein folding in eukaryotes. mechanisms and consequences J. Cell Biol. 164:2004;341-346
47. Tu B.P., Ho-Schleyer S.C., Travers K.J., Weissman J.S. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science. 290:2000;1571-1574
48. Van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229:1993;105-124