NMR solution structure of subunit F of the methanogenic A 1A O adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B

Biochemistry

Volumn 46, Issue 42, 2007, Pages 11684-11694

  Gayen, Shovanlal ^a,b   Vivekanandan, Subramanian ^a   Biuković, Goran ^a,b   Grüber, Gerhard ^a,b   Ho, Sup Yoon ^a  

^a NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

^b Section of Structure and Function of Molecular Motors   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE (ATP) SYNTHASE; FLUORESCENCE SIGNALS; METHANOSARCINA MAZEI; MUTANT SUBUNITS;

BINDING ENERGY; FLUORESCENCE; MOLECULAR INTERACTIONS; MOLECULAR STRUCTURE; MUTAGENESIS; NUCLEOTIDES;

ENZYMES;

A1A0 ADENOSINE TRIPHOSPHATE SYNTHASE; ADENOSINE TRIPHOSPHATE; AMINO ACID; ISOLEUCINE; NUCLEOTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; DYNAMICS; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SUBUNIT; METHANOSARCINA; METHANOSARCINA MAZEI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ATP SYNTHETASE COMPLEXES; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; METHANOSARCINA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEOTIDES; PLIABILITY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE; SPECTRUM ANALYSIS, RAMAN; TRYPTOPHAN;

METHANOSARCINA MAZEI; PUFFINUS AURICULARIS;

EID: 35448976143     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701102n     Document Type: Article

References (43)

1. Schäfer, G., Engelhard, M., and Müller, V. (1999) Bioenergetics of the archaea, Mol. Biol. Rev. 63, 570-620.
2. Müller, V., Lingl, A., Coskun, Ü., and Grüber, G. (2005) Functional and structural modules of the A-type ATP synthase, J. Mol. Microbiol. Biotechnol. 10, 167-180.
3. 0-ATP synthase, FEBS Lett. 545, 61-70.
4. Forgac, M. (2000) Structure, mechanism and regulation of the clathrin-coated vesicle and yeast vacuolar H(+)-ATPases, J. Exp. Biol. 203, 71-80.
5. Lolkema, J. S., Chaban, Y., and Boekema, E. J. (2003) Subunit composition, structure, and distribution of bacterial V-type AT-Pase, J. Bioenerg. Biomembr. 35, 323-336.
6. Muller, V., and Grüber, G. (2003) ATP syntases: structure, function and evolution of unique energy converters, Cell Mol. Life Sci. 60, 474-494.
7. 1 ATPase from the archaeon, Methanosarcina mazei Göl, Biochemistry 40, 1890-1896.
8. Maegawa, Y., Morita, H., Iyaguchi, D., Yao, M., Watanabe, N., and Tanaka, I. (2006) Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk, Acta Crystallogr. D62, 483-488.
9. O subunits A and B, J. Mol. Biol. 358, 725-740.
10. 1-ATPase from Methanosarcina mazei Göl, J. Biol. Chem. 279, 22759-22764.
11. Coskun, Ü., Grüber, G., Koch, M. H. J., Godovac-Zimmermann, J., Lemker, T., and Müller, V. (2002) Cross-talk in the A1-ATPase from Methanosarcina mazei Göl due to nucleotide binding, J. Biol. Chem. 277, 17327-17333.
12. O ATPsynthase, J. Bioenerg. Biomembr. 38, 83-92.
13. Coskun, U., Chaban, Y. L., Lingl, A., Müller, V., Keegstra, W., Boekema, E. J., and Grüber, G. (2004) Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jannaschii visualized by electron microscopy, J. Biol. Chem. 279, 38644-38648.
14. Bernal, R. A., and Stock, D. (2004) Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy, Structure 12, 1789-1798.
15. +-ATPase, J. Mol. Biol. 366, 933-944.
16. O ATP synthase from Methanocaldococcus jannaschii and its binding to the catalytic A subunit, Biochemistry 46, 2070-2078.
17. O ATPase from the archaeon Methanosarcina mazei Göl, J. Biol. Chem. 271, 18843-18852.
18. Gibbons, C., Montgomery, M. G., Leslie, A. G., and Walker, J. E. (2000) The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution, Nat. Struct. Biol. 7, 1055-1061.
19. 1 ATPase by disulfide bond formation. A state of the enzyme with all three catalytic sites open and with equal low affinity for nucleotides, FEBS Lett. 426, 37-40.
20. 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis, Cell 106, 331-341.
21. 1 ATPase, EMBO J. 25, 5433-5442.
22. 1-ATP synthase, Biochim. Biophys. Acta 1757, 326-338.
23. Wilkens, S., Dahlquist, F. W., McIntosh, L. P., Donaldson, L. W., and Capaldi, R. A. (1995) Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy, Nat. Struct. Biol. 2, 961-967.
24. Makyio, H., Iino, R., Ikeda, C., Imamura, H., Tamakoshi, M., Iwata, M., Stock, D., Bernal, R. A., Carpenter, E. P., Yoshida, M., Yokoyama, K., and Iwata, S. (2005) Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus, EMBO J. 24, 3974-3983.
25. Crivici, A., and Ikura, M. (1995) Molecular and structural basis of target recognition by calmodulin, Annu. Biophys. Biomol. Struct. 24, 85-116.
26. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
27. Kneller, D. G., and Goddard, T. D. (1997) SPARKY, 3.105 ed., University of California, San Francisco, CA.
28. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York.
29. Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
30. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy, Biochemistry 31, 1647-1651.
31. Guntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the pew program DYANA, J. Mol. Biol. 273, 283-298.
32. Herrmann, T., Guntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA, J. Mol. Biol. 319, 209-227.
33. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
34. Shaka, A. J., Barker, P. B., and Freeman, R. (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation, J. Magn. Reson. 64, 547-552.
35. 15N labelled homeodomain and its DNA complex, J. Am. Chem. Soc. 119, 3842-3843.
36. Loria, J. P., Rance, M., and Palmer, A. G. (1999) A relaxation- compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy, J. Am. Chem. Soc. 121, 2331-2332.
37. Gallopin, M., Ochsenbein, F., Guittet, E., and Heijenoort, C. V. (2004) Analysis of slow motions in the micro-millisecond range on domain 1 of annexin I, C. R. Acad. Sci., Ser. IIc: Chim. 7, 253-258.
38. Delaglio, F., Grzesiek. S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX, J. Biomol. NMR 6, 277-293.
39. Kneller, D. G., and Goddard, T. D. (1997) SPARKY, 3.105 ed., University of California, San Francisco, CA.
40. Cavanagh, J. (1996) Referencing, Protein NMR spectroscopy: Principles and practice, p 175, Academic Press, San Diego.
41. 15N NMR relaxation, Biochemistry 33, 5984-6003.
42. Merritt, E. A., and Murphy, M. E. (1997) Raster3D Version 2.0. A program for photorealistic molecular graphics, Acta Crystallogr. D50, 869-873.
43. Gibbons, C., Montgomery, M. G., Leslie, A. G., and Walker, J. E. (2000) The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution, Nat. Struct. Biol. 7, 1055-1061.