2f43: Difference between revisions

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[[Image:2f43.gif|left|200px]]
{{Seed}}
[[Image:2f43.png|left|200px]]


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{{STRUCTURE_2f43|  PDB=2f43  |  SCENE=  }}  
{{STRUCTURE_2f43|  PDB=2f43  |  SCENE=  }}  


'''Rat liver F1-ATPase'''
===Rat liver F1-ATPase===




==Overview==
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ATP synthesis from ADP, P(i), and Mg2+ takes place in mitochondria on the catalytic F1 unit (alpha3beta3gammedeltaepsilon) of the ATP synthase complex (F0F1), a remarkable nanomachine that interconverts electrochemical and mechanical energy, producing the high energy terminal bond of ATP. In currently available structural models of F1, the P-loop (amino acid residues 156GGAGVGKT163) contributes to substrate binding at the subunit catalytic sites. Here, we report the first transition state-like structure of F1 (ADP.V(i).Mg.F1) from rat liver that was crystallized with the phosphate (P(i)) analog vanadate (VO(3-)4 or V(i)). Compared with earlier "ground state" structures, this new F1 structure reveals that the active site region has undergone significant remodeling. P-loop residue alanine 158 is located much closer to V(i) than it is to P(i) in a previous structural model. No significant movements of P-loop residues of the subunit were observed at its analogous but noncatalytic sites. Under physiological conditions, such active site remodeling involving the small hydrophobic alanine residue may promote ATP synthesis by lowering the local dielectric constant, thus facilitating the dehydration of ADP and P(i). This new crystallographic study provides strong support for the catalytic mechanism of ATP synthesis deduced from earlier biochemical studies of liver F1 conducted in the presence of V(i) (Ko, Y. H., Bianchet, M., Amzel, L. M., and Pedersen, P. L. (1997) J. Biol. Chem. 272, 18875-18881; Ko, Y. H., Hong, S., and Pedersen, P. L. (1999) J. Biol. Chem. 274, 28853-28856).
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{{ABSTRACT_PUBMED_16531409}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism., Chen C, Saxena AK, Simcoke WN, Garboczi DN, Pedersen PL, Ko YH, J Biol Chem. 2006 May 12;281(19):13777-83. Epub 2006 Mar 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16531409 16531409]
Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism., Chen C, Saxena AK, Simcoke WN, Garboczi DN, Pedersen PL, Ko YH, J Biol Chem. 2006 May 12;281(19):13777-83. Epub 2006 Mar 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16531409 16531409]
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis., Bianchet MA, Hullihen J, Pedersen PL, Amzel LM, Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11065-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9736690 9736690]
The three-dimensional structure of rat liver mitochodria F1-ATPase: X-ray diffraction studies., Bianchet M, Medjahed D, Hulihen J, Pedersen PL, Amzel LM, Biochim Biophys Acta. 1994 Aug 30;1187(2):163-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8075110 8075110]
Quaternary structure of ATP synthases: symmetry and asymmetry in the F1 moiety., Amzel LM, Bianchet MA, Pedersen PL, J Bioenerg Biomembr. 1992 Oct;24(5):429-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1429535 1429535]
Mitochondrial ATP synthase. Quaternary structure of the F1 moiety at 3.6 A determined by x-ray diffraction analysis., Bianchet M, Ysern X, Hullihen J, Pedersen PL, Amzel LM, J Biol Chem. 1991 Nov 5;266(31):21197-201. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1834656 1834656]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Oxidative phosphorylation]]
[[Category: Oxidative phosphorylation]]
[[Category: Vanadate]]
[[Category: Vanadate]]
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