Structure at 2.3 Å resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment

Structure

Volumn 8, Issue 6, 2000, Pages 669-684

  Hunte, Carola ^a   Koepke, Juergen ^a   Lange, Christian ^a   Roßmanith, Tanja ^a   Michel, Hartmut ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

Coenzyme Q6; Matrix processing peptidase; Proton transfer; Stigmatellin; Yeast cytochrome bc1 complex

Indexed keywords

UBIQUINOL CYTOCHROME C REDUCTASE;

ARTICLE; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTON TRANSPORT; SACCHAROMYCES CEREVISIAE; STRUCTURE ANALYSIS;

SACCHAROMYCES CEREVISIAE;

EID: 0034660152     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00152-0     Document Type: Article

References (52)

1. Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Ann. Rev. Biochem. 54:1985;1015-1069.
2. Brandt U., Trumpower B.L. The proton motive Q-cycle in mitochondria and bacteria. CRC Crit. Rev. Biochem. 29:1994;165-197.
3. 1 complex from beef heart. Methods Enzymol. 126:1986;224-237.
4. de Vries S., Marres S.A.M. The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim. Biopys. Acta. 895:1987;205-239.
5. 1 complex. J. Biol. Chem. 269:1994;12 947-12 957.
6. 1 complex from bovine heart mitochondria. Science. 277:1997;60-66.
7. 1. Nature. 392:1998;677-684.
8. 1 complex. Science. 281:1998;64-71.
9. 1 complex determined by MAD phasing at 1.5 Å resolution. Structure. 4:1996;567-579.
10. Mitchell P. Possible molecular mechanisms of the protonmotive function of cytochrome systems. J. Theor. Biol. 62:1976;327-367.
11. Crofts A.R. The mechanism of ubiquinol:cytochrome c oxidoreductases of mitochondria and of Rhodopseudomonas sphaeroides. Martonosi A.N. The Enzymes of Biological Membranes. 1985;347-382 Plenum Publishing Corporation, New York.
12. 1 complex from bovine heart. Proc. Natl Acad. Sci. USA. 95:1998;8026-8033.
13. 1 complex. Biochim. Biophys. Acta. 1275:1996;61-69.
14. Ostermeier C., Iwata S., Ludwig B., Michel H. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nat. Struct. Biol. 2:1995;842-846.
15. Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
16. Ostermeier C., Harrenga A., Ermler U., Michel H. Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment. Proc. Natl Acad. Sci. USA. 94:1997;10 547-10 553.
17. 1 complex into yeast mitochondria. J. Biol. Chem. 265:1990;16 541-16 547.
18. 1 complex from Saccharomyces cerevisiae studied using hybrid complexes. Eur. J. Biochem. 249:1997;762-769.
19. 1-c. J. Biol. Chem. 260:1991;5392-5398.
20. 1-c complex. Isolation, purification, and properties. J. Biol. Chem. 258:1983;13 543-13 551.
21. Kim C.H., Balny C., King Z. Role of the hinge protein in the electron transfer between cardiac cytochrome c1 and c. Equilibrium constants and kinetic probes. J. Biol. Chem. 262:1987;8103-8108.
22. 1 complex in Saccharomyces cerevisiae. J. Biol. Chem. 265:1990;17 005-17 011.
23. Rawlings N.D., Barrett A.J. Homologues of insulinase, a new superfamily of metallopeptidases. Biochem. J. 275:1991;389-391.
24. Yang M., Jensen R.E., Yaffe M.P., Oppliger W., Schatz G. Import of proteins into yeast mitochondria: the purified matrix processing protease contains two subunits which are encoded by nuclear MAS1 and MAS2 genes. EMBO J. 7:1988;3857-3862.
25. Braun H-P., Emmermann M., Kruft V., Schmitz U.K. The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J. 11:1992;3219-3227.
26. Schulte U., Arretz M., Schneider H., Tropschug M., Wachter E., Neupert W., Weiss H. A family of mitochondrial proteins involved in bioenergetics and biogenesis. Nature. 339:1989;147-149.
27. 1 complex of bovine heart mitochondria. J. Biol. Chem. 273:1998;20 752-20 757.
28. Tzagaloff A., Wu M., Crivellone M. Assembly of the mitochondrial membrane system. Characterization of COR1, the structural gene for the 44-kilodalton core protein of yeast coenzyme QH2-cytochrome c reductase. J. Biol. Chem. 261:1986;17 163-17 169.
29. Oudshoorn P., Van Steeg H., Swinkels B.W., Schoppink P., Grivell L.A. Subunit II of the genes encoding the 40 kD subunit II or the 17 kD subunit VI on the steady-state kinetics of yeast ubiquinol-cytochrome-c oxidoreductase. Nucleotide sequence of the gene and features of the protein. Eur. J. Biochem. 163:1997;97-103.
30. 1 complex evolutionary relics of a processing protease? Trends Biochem. Sci. 20:1995;171-174.
31. 1 complex in Saccharomyces cerevisiae. J. Biol. Chem. 272:1997;4699-4704.
32. Lancaster C.R.D., Michel H. The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB. Structure. 5:1997;1339-1359.
33. 1 complex. FEBS Lett. 412:1997;257-264.
34. 1 complex. Proc. Natl Acad. Sci. USA. 96:1999;10 021-10 026.
35. Degli Esposti M., De Vries S., Crimi M., Ghelli A., Patarnello T., Meyer A. Mitochondrial cytochrome b: evolution and structure of the protein. Biochim. Biophys. Acta. 1143:1993;243-271.
36. Berry E.A., Huang L., DeRose V.J. Ubiquinol-cytochrome c oxidoreductase of higher plants. J. Biol. Chem. 266:1991;9064-9077.
37. Kleymann G., Ostermeier C., Ludwig B., Skerra A., Michel H. Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes. Bio/Technol. 13:1995;155-160.
38. Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend: Data Collection and Processing. 1993;56-62 SERC Daresbury Laboratory, Warrington, UK.
39. Minor, W. (1993). XDISPLAYF Program. Purdue University.
40. The CCP4 suit: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
41. Brünger A.T. X-PLOR, Version 3.1: a system for X-ray crystallography and NMR. 1992;Yale University Press, New Haven, CT.
42. Brünger A.T. Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Crystallog. A. 38:1990;46-57.
43. Cowtan K. 'dm': an automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. 31:1994;34-38.
44. Lamzin V.S., Wilson K.S. Automated refinement of protein models. Acta Crystallogr. D. 49:1993;129-149.
45. McRee D.E. Practical Protein Crystallography. 1993;Academic Press Inc.
46. Jones A., Zou J-Y., Cowan S., Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of error in these models. Acta Crystallogr. A. 47:1991;110-119.
47. Brünger A.T., Warren G.L.et al. Crystallographic and NMR system: a new software suite of macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
48. Brünger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 335:1992;472-474.
49. Costanzo M.C., Garrels J.I.et al. The yeast proteome Database (YPD) and Caenorhabditis elegans proteome database (WormPD): comprehensive resources for the organization and comparison of model organism protein information. Nucleic Acids Res. 28:2000;73-76.
50. Holm L., Sander C. Mapping the protein universe. Science. 273:1996;595-602.
51. Humphrey, W.F., Dalke, A., & Schulten, K. (1996) VMD: Visual Molecular Dynamics. J. Mol. Graph. 14, 33-8, 27-8.
52. Ippolito J.A., Alexander R.S., Christianson D.W. Hydrogen bond stereochemistry in protein structure and function. J. Mol. Biol. 215:1990;457-471.