The structure of bovine F1-ATPase in complex with its regulatory protein IF1

Nature Structural Biology

Volumn 10, Issue 9, 2003, Pages 744-750

  Cabezón, Elena ^a,c   Montgomery, Martin G ^a   Leslie, Andrew G W ^b   Walker, John E ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^c UNIVERSITY OF CANTABRIA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN IF1; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REGULATOR PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; ATPASE INHIBITORY PROTEIN; PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; CATTLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; STEREOCHEMISTRY; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; HYDROLYSIS; METABOLISM; MITOCHONDRION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

BOS TAURUS; BOVINAE;

ADENOSINE TRIPHOSPHATE; ANIMALS; CATTLE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HYDROLYSIS; MITOCHONDRIA; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEINS; PROTON-TRANSLOCATING ATPASES;

EID: 0041819514     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb966     Document Type: Article

References (41)

1. Boyer, P.D. The ATP synthase: a splendid molecular machine, Annu. Rev. Biochem. 66, 717-749 (1997).
2. Walker, J.E. ATP synthesis by rotary catalysis (Nobel lecture). Angew. Chem. Int. Edn. Engl. 37, 2309-2319 (1998).
3. c-ATP synthase. Biochim. Biophys. Acta 1553, 188-211 (2002).
4. 1-ATPase and in its absence, J. Mol. Biol. 242, 408-421 (1994).
5. Karrasch, S. & Walker, J.E. Novel features in the structure of bovine ATP synthase. J. Mol. Biol. 290, 379-384 (1999).
6. Rubinstein, J. & Walker, J.E. ATP synthase from Saccharomyces cerevisiae: location of the OSCP subunit in the peripheral stalk region. J. Mol. Biol. 321, 613-619 (2002).
7. Stock, D., Leslie, A.G.W. & Walker, J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705 (1999).
8. 1-ATPase at 2.4 Å resolution. Nat. Struct, Biol, 7, 1055-1061 (2000).
9. 1-ATPase from bovine heart mitochondria. Nature 370, 621-628 (1994).
10. Pullman, M.E. & Monroy, G.C. A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity. J. Biol. Chem. 238, 3762-3769 (1963).
11. 0-ATPase. Biochim. Biophys. Acta 1458, 343-355 (2000).
12. van Raaij, M.J. et al. The ATPase inhibitor protein from bovine heart mitochondria: the minimal inhibitory sequence. Biochemistry 35, 15618-15625 (1996).
13. 1-ATPase. J. Mol. Biol. 308, 325-339 (2001).
14. 1-ATPase. EMBO J. 20, 6990-6996 (2001).
15. 1. J. Biol. Chem. 275, 28353-28355 (2000).
16. 1, by pH. J. Biol. Chem. 275, 25460-25464 (2000).
17. Rouslin, W. Protonic inhibition of the mitochondrial oligomycin-sensitive adenosine 5′-triphosphatase in ischemic and autolyzing cardiac muscle. Possible mechanism for the mitigation of ATP hydrolysis under nonenergizing conditions. J. Biol. Chem. 258, 9657-9661 (1983).
18. Rouslin, W. Factors affecting the reactivation of the oligomycin-sensitive adenosine 5′-triphosphatase and the release of ATPase inhibitor protein during the re-energization of intact mitochondria from ischemic cardiac muscle. J. Biol. Chem. 262. 3472-3476 (1987).
19. + symport, J. Biol. Chem. 264, 15224-15229 (1989).
20. 0-ATPase upon de-energization of mitochondria. J. Biochem. (Tokyo) 113, 350-354 (1993).
21. 1 β-subunit. FEBS Lett. 229, 224-228 (1988).
22. 1-ATPase, from ox heart mitochondria with its naturally occurring inhibitor protein. Studies using radio-iodinated inhibitor protein. Biochim. Biophys. Acta 724, 128-141 (1983).
23. Milgrom, Y.M. When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites. Eur. J. Biochem. 200, 789-795 (1991).
24. 1 during adenosine 5′-triphosphate synthesis activation or hydrolysis: role of protein inhibitor and hysteretic inhibition. Biochemistry 27, 8969-8974 (1988).
25. +-ATPases. Curr. Top. Bioenerg. 11, 149-199 (1981).
26. Boyer, P.D. The binding change mechanism for ATP synthase: some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250 (1993).
27. 1-ATPase residue α-Arg376 for catalytic transition state stabilisation. Biochemistry 38, 15493-15499 (1999).
28. 1-ATPases. J. Biol. Chem. 277, 41334-41341 (2002).
29. Klionsky, D.J., Bruslow, W.S.A. & Simoni, R.D. In vivo evidence for the role of the ε-subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160, 1055-1060 (1985).
30. 1-ATPase revealed by a 4.4 Å resolution map obtained by X-ray crystallography. Proc. Natl. Acad. Sci. USA 96, 13697-13702 (1999).
31. Rodgers, A.J. & Wilce, M.C. Structure of the γ-ε complex of ATP synthase. Nat. Struct. Biol. 7, 1051-1054 (2000).
32. 1-ATPase. J. Biol. Chem. 276, 47227-47232 (2001).
33. 0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme. Proc. Natl. Acad. Sci. USA 98, 6560-6564 (2001).
34. 1-ATPase. Structural implications and functional consequences. J. Biol. Chem. 270, 9185-9191 (1995).
35. Leslie, A.W.G. Joint CCP4 and ESF-EACMB Newsletter on Protein Crystallography Vol. 26 (Daresbury Laboratory, Warrington, UK, 1992).
36. Collaborative Computational Project, Number 4. The CCP4 Suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
37. Navaza, J. AmoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
38. 2+ ADP and aluminum fluoride. Structure 8, 567-573 (2000).
39. Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. A 54, 905-921 (1998).
40. 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. Crystallogr. 26, 283-291 (1993).
41. Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15, 132-134 (1997).