Crossref journal-article
Elsevier BV
Cell (78)
Bibliography

Menz, R. I., Walker, J. E., & Leslie, A. G. W. (2001). Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites. Cell, 106(3), 331–341.

Authors 3
  1. R.Ian Menz (first)
  2. John E. Walker (additional)
  3. Andrew G.W. Leslie (additional)
References 46 Referenced 407
  1. 10.1038/370621a0 / Nature / Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria by Abrahams (1994)
  2. 10.1016/0014-5793(94)00588-5 / FEBS Lett. / Spatial precision of a catalytic carboxylate of F1-ATPase Beta-subunit probed by introducing different carboxylate-containing side-chains by Amano (1994)
  3. 10.1074/jbc.271.30.18128 / J. Biol. Chem. / Catalytic activities of α3β3γ complexes of F1-ATPase with 1, 2, or 3 incompetent catalytic sites by Amano (1996)
  4. 10.1016/0005-2728(93)90063-L / Biochim. Biophys. Acta / The binding change mechanism for ATP synthase—some probabilities and possibilities by Boyer (1993)
  5. 10.1146/annurev.biochem.66.1.717 / Annu. Rev. Biochem. / The ATP synthase—a splendid molecular machine by Boyer (1997)
  6. 10.1016/S0005-2728(00)00077-3 / Biochim. Biophys. Acta / Catalytic site forms and controls in ATP synthase catalysis by Boyer (2000)
  7. 10.1016/S0969-2126(00)00145-3 / Structure / Structure of bovine mitochondrial F1-ATPase inhibited by Mg2+ ADP and aluminium fluoride by Braig (2000)
  8. 10.1107/S0907444994003112 / Acta Crystallogr. D Biol. Crystallogr. / The CCP4 Suite (1994)
  9. 10.1016/S0021-9258(18)33684-6 / J. Biol. Chem. / Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites by Cross (1982)
  10. 10.1146/annurev.micro.50.1.791 / Annu. Rev. Microbiol. / The F0F1-type ATP synthases of bacteria by Deckers-Hebestreit (1996)
  11. 10.1021/bi962353+ / Biochemistry / ADP-fluoroaluminate complexes are formed cooperatively at two catalytic sites of wild-type and mutant α3β3γ subcomplexes of the F1ATPase from the thermophilic Bacillus PS3 by Dou (1997)
  12. 10.1073/pnas.92.24.10964 / Proc. Natl. Acad. Sci. USA / Rotation of subunits during catalysis by Escherichia coli F1-ATPase by Duncan (1995)
  13. 10.1016/S0021-9258(19)39579-1 / J. Biol. Chem. / Thermodynamic analyses of the catalytic pathway of F1-ATPase from Escherichia coli—implications regarding the nature of energy coupling by F1-ATPases by El-Shawi (1990)
  14. 10.1016/S1093-3263(97)00021-1 / J. Mol. Graph. Model. / An extensively modified version of MolScript that includes greatly enhanced coloring capabilities by Esnouf (1997)
  15. 10.1016/S0021-9258(17)44153-6 / J. Biol. Chem. / The synthesis of ATP by the membrane-bound ATP synthase complex from medium 32Pi under completely uncoupled conditions by Feldman (1983)
  16. {'key': '10.1016/S0092-8674(01)00452-4_BIB16', 'series-title': 'Structure and Mechanism in Protein Science', 'author': 'Fersht', 'year': '1998'} / Structure and Mechanism in Protein Science by Fersht (1998)
  17. 10.1038/80981 / Nat. Struct. Biol. / The structure of the central stalk in bovine F1-ATPase at 2.4 A resolution by Gibbons (2000)
  18. 10.1021/bi00233a013 / Biochemistry / Fluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymatic mechanism of the mitochondrial F1-ATPase by Issartel (1991)
  19. 10.1107/S0108767390010224 / Acta Crystallogr. A / Improved methods for binding protein models in electron density maps and the location of errors in these models by Jones (1991)
  20. 10.1107/S0021889892009944 / J. Appl. Cryst. / PROCHECK—a program to check the stereochemical quality of protein structures by Laskowski (1993)
  21. 10.1021/bi992530h / Biochemistry / Escherichia coli ATP synthase alpha subunit Arg-376 by Le (2000)
  22. {'key': '10.1016/S0092-8674(01)00452-4_BIB22', 'series-title': 'Joint CCP4 and EACMB Newsletter Protein Crystallography', 'author': 'Leslie', 'year': '1992'} / Joint CCP4 and EACMB Newsletter Protein Crystallography by Leslie (1992)
  23. 10.1074/jbc.272.6.3648 / J. Biol. Chem. / F1-ATPase, roles of three catalytic site residues by Lobau (1997)
  24. 10.1006/jmbi.1993.1081 / J. Mol. Biol. / Crystallisation of F1-ATPase from bovine heart mitochondria by Lutter (1993)
  25. 10.1242/jeb.203.1.1 / J. Exp. Biol. / Rotation of F1-ATPase and the hinge residues of the beta subunit by Masaike (2000)
  26. 10.1146/annurev.arplant.51.1.83 / Annu. Rev. Plant Physiol. Plant Mol. Biol. / The chloroplast ATP synthase by McCarty (2000)
  27. 10.1107/S0907444996012255 / Acta Crystallogr. D Biol. Crystallogr. / Refinement of macromolecular structures by the maximum-likelihood method by Murshudov (1997)
  28. 10.1021/bi990663x / Biochemistry / The role of βArg-182, an essential catalytic site residue in Escherichia coli F1-ATPase by Nadanaciva (1999)
  29. 10.1021/bi9917683 / Biochemistry / Importance of F1-ATPase residue αArg-376 for catalytic transition state stabilization by Nadanaciva (1999)
  30. 10.1021/bi000941o / Biochemistry / New probes of the F1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously by Nadanaciva (2000)
  31. 10.1107/S0108767393007597 / Acta Crystallogr. A / AMoRe by Navaza (1994)
  32. 10.1038/386299a0 / Nature / Direct observation of the rotation of F1-ATPase by Noji (1997)
  33. 10.1016/S0005-2728(00)00075-X / Biochim. Biophys. Acta / On what makes the γ-subunit spin during ATP hydrolysis by F1 by Ren (2000)
  34. 10.1038/80975 / Nat. Struct. Biol. / Structure of the gamma-epsilon complex of ATP synthase by Rodgers (2000)
  35. 10.1016/S0021-9258(17)40483-2 / J. Biol. Chem. / Evidence for energy-dependent change in phosphate binding for mitochondrial oxidative phosphorylation based on measurements of medium and intermediate phosphate-water exchanges by Rosing (1977)
  36. 10.1038/381623a0 / Nature / Intersubunit rotation in active F-ATPase by Sabbert (1996)
  37. 10.1126/science.286.5445.1700 / Science / Molecular architecture of the rotary motor in ATP synthase by Stock (1999)
  38. {'key': '10.1016/S0092-8674(01)00452-4_BIB38', 'series-title': 'Biochemistry', 'author': 'Stryer', 'year': '1995'} / Biochemistry by Stryer (1995)
  39. 10.1107/S0108767387099124 / Acta Crystallogr. A / An efficient general-purpose least-squares refinement program for macromolecular structures by Tronrud (1987)
  40. 10.1074/jbc.274.9.5701 / J. Biol. Chem. / Cross-linking of two beta subunits in the closed conformation in F1-ATPase by Tsunoda (1999)
  41. 10.1002/(SICI)1521-3773(19980918)37:17<2308::AID-ANIE2308>3.0.CO;2-W / Angew. Chem. Int. Ed. Engl. / ATP synthesis by rotary catalysis (Nobel Lecture) by Walker (1998)
  42. 10.1016/S0005-2728(96)00121-1 / Biochim. Biophys. Acta / Catalytic mechanism of F1-ATPase by Weber (1997)
  43. 10.1016/S0005-2728(00)00082-7 / Biochim. Biophys. Acta / ATP synthase by Weber (2000)
  44. 10.1074/jbc.271.31.18711 / J. Biol. Chem. / Specific tryptophan substitution in catalytic sites of Escherichia coli F1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysis by Weber (1996)
  45. 10.1016/S0021-9258(20)80703-0 / J. Biol. Chem. / Specific placement of tryptophan in the catalytic sites of Escherichia-coli F1-ATPase provides a direct probe of nucleotide-binding—maximal ATP hydrolysis occurs with 3 sites occupied by Weber (1993)
  46. 10.1038/35073513 / Nature / Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase by Yasuda (2001)
Dates
Type When
Created 21 years, 4 months ago (April 15, 2004, 5:36 a.m.)
Deposited 2 years, 6 months ago (Jan. 25, 2023, 5:45 p.m.)
Indexed 3 days, 14 hours ago (Aug. 19, 2025, 6:15 a.m.)
Issued 24 years ago (Aug. 1, 2001)
Published 24 years ago (Aug. 1, 2001)
Published Print 24 years ago (Aug. 1, 2001)
Funders 0

None

@article{Menz_2001, title={Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites}, volume={106}, ISSN={0092-8674}, url={http://dx.doi.org/10.1016/s0092-8674(01)00452-4}, DOI={10.1016/s0092-8674(01)00452-4}, number={3}, journal={Cell}, publisher={Elsevier BV}, author={Menz, R.Ian and Walker, John E. and Leslie, Andrew G.W.}, year={2001}, month=aug, pages={331–341} }