Crystal structure of the ε subunit of the proton-translocating ATP synthase from Escherichia coli

Structure

Volumn 5, Issue 9, 1997, Pages 1219-1230

  Uhlin, Ulla ^a,c   Cox, Graeme B ^b   Guss, J Mitchell ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

^b Australian National University   (Australia)

^c SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

Author keywords

ATP synthase; ATPase; Crystal structure; subunit

Indexed keywords

ESCHERICHIA COLI;

PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; HYDROGEN BOND; MITOCHONDRION; MOLECULAR GENETICS; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MITOCHONDRIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTON-TRANSLOCATING ATPASES; PROTONS; SEQUENCE ALIGNMENT;

EID: 0030611634     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00272-4     Document Type: Article

References (45)

1. Senior, A.E. (1990). The proton-translocating ATPase of Escherichia coli. Annu. Rev. Biophys. Biophys. Chem. 19, 7-41.
2. +-translocating ATP syntheses. In The Bacteria: a Treatise on Structure and Function. (Krulwich, T.A., ed.), pp. 345-391, Academic Press, Inc, New York, NY, USA.
3. Boyer, P.D. (1993). The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250.
4. Pedersen, P.L. (1996). Frontiers in ATP synthase research: understanding the relationship between subunit movements and ATP synthesis. J. Bioenerg. Biomembr. 28, 389-395.
5. 1 moiety at 3.6 À determined by X-ray diffraction analysis. J. Biol. Chem. 266, 21197-21201.
6. 1-ATPase from bovine heart mitochondria. Nature 370, 621-628.
7. 1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Structure 5, 825-836.
8. Boyer, P.D. (1989). A perspective of the binding change mechanism for ATP synthesis. FASEB J 3, 2164-2178.
9. Duncan, T.M., Bulygin, V.V., Zhou, Y., Hutcheon, M.L. & Cross, R.L. (1995). Rotation of subunits during catalysis by Escherichia coli F1-ATPase. Proc. Natl. Acad. Sci. USA 92, 10964-10968.
10. 1-ATPase. Nature 386, 299-302.
11. Sternweis, P.C. & Smith, J.B. (1980). Characterization of the inhibitory (ε) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli. Biochemistry 19, 526-531.
12. Mendel-Hartvig, J. & Capaldi, R.A. (1991). Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the ε subunit in Escherichia coli adenosinetriphosphatase. Biochemistry 30, 1278-1284.
13. Sternweis, P.C. (1978). The ε subunit of Escherichia coli coupling factor 1 is required for its binding to the cytoplasmic domain. J. Biol. Chem. 253, 3123-3128.
14. Skakoon, E.N. & Dunn, S.D. (1993). Orientation of the ε subunit in Escherichia coli ATP synthase. Arch. Biochem. Biophys. 302, 279-284.
15. Skakoon, E.N. & Dunn, S.D. (1993). Location of conserved residue histidine-38 of the ε subunit of Escherichia Coli ATP synthase. Arch. Biochem. Biophys. 302, 272-278.
16. 0 parts and can interact with both the ε and c oligomer. J. Biol. Chem. 271, 28341-28347.
17. 0 subunit c. J. Biol. Chem. 270, 24609-24619.
18. 1-ATPase. J. Biol. Chem. 267, 18953-18960.
19. 1-ATPase. Structural implications and functional consequences. J. Biol. Chem. 270, 9185-9191.
20. 0-type ATPase. J. Biol. Chem. 271, 13888-13891.
21. 0-type ATPase during energy coupling. J. Bioenerg. Biomembr. 28, 397-401.
22. Wilkens, S., Dahlquist, F.W., McIntosh, L.P., Donaldson, L.W. & Capaldi, R.A. (1995). Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat. Struct Biol. 2, 961-967.
23. Wilkens, S., Dunn, S.D., Chandler, J., Dahlquist, F.W. & Capaldi, R.A. (1997). Solution structure of the N-terminal domain of the δ subunit of the E. coli ATP synthase. Nat. Struct. Biol. 4, 198-201.
24. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matches. J. Mol. Biol. 233, 123-138.
25. Sheriff, S., Hendrickson, W.A. & Smith, J.L. (1987). Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J. Mol. Biol. 197, 273-296.
26. Smith, J.B. & Sternweis, P.C. (1977). Purification membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphate from Escherichia coli. Biochemistry 16, 306-311.
27. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. & Lipman, D.J. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
28. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
29. 0). J. Biol. Chem. 263, 17437-17422.
30. 1). Arch. Biochem. Biophys. 292, 87-94.
31. 0-ATPase of Escherichia coli. Biochim. Biophys. Acta 890, 195-204.
32. 0 ATP synthase affect its inhibitory properties. J. Bacteriol. 174, 633-637.
33. Aggeler, R., Weinreich, F. & Capaldi, R.A. (1995). Arrangement of the ε subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit. Biochim. Biophys. Acta 1230, 62-68.
34. 1 ATPase, modification of these sites with tetrafluorophenyl azidemaleimides, and examination of changes in the binding of the ε subunit when different nucleotides are in catalytic sites. Biochemistry 31, 2956-2961.
35. 1-ATPase. J. Biol. Chem. 271, 3081-3024.
36. 1 portion of the ATPase of Escherichia coli. J. Mol. Biol. 228, 306-309.
37. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S.S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
38. Collaborative Computational Project no. 4. (1994). Acta Cryst D 50, 760-763.
39. Brünger, A.T. (1992). X-PLOR, Version 3.1, A System for Crystallography and NMR. Yale University Press, New Haven, CT, USA.
40. Kleywegt, G.J. & Jones, T.A. (1996). Phi/Psi-chology: Ramachandran revisited. Structure 4, 1395-1400.
41. Engh, R.A. & Huber, R. (1991). Accurate bond length and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
42. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Cryst. 24, 946-950.
43. Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: graphical representation and analysis of surface properties. Biophys. J. 64, 166-170.
44. Bairoch, A. & Boeckmann, B. (1994). The SWISS-PROT protein sequence data bank: current status. Nucl. Acid Res. 19, 3578-3580.
45. Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.