2hld
Crystal structure of yeast mitochondrial F1-ATPase
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OverviewOverview
The crystal structure of yeast mitochondrial F(1) ATPase contains three, independent copies of the complex, two of which have similar conformations, while the third differs in the position of the central stalk relative to, the alpha(3)beta(3) sub-assembly. All three copies display very similar, asymmetric features to those observed for the bovine enzyme, but the yeast, F(1) ATPase structures provide novel information. In particular, the, active site that binds ADP in bovine F(1) ATPase has an ATP analog bound, and therefore this structure does not represent the ADP-inhibited form. In, addition, one of the complexes binds phosphate in the nucleotide-free, catalytic site, and comparison with other structures provides a picture of, the movement of the phosphate group during initial binding and subsequent, catalysis. The shifts in position of the central stalk between two of the, three copies of yeast F(1) ATPase and when these structures are compared, to those of the bovine enzyme give new insight into the conformational, changes that take place during rotational catalysis.
About this StructureAbout this Structure
2HLD is a Protein complex structure of sequences from Saccharomyces cerevisiae with MG, PO4 and ANP as ligands. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
ReferenceReference
Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase., Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM, EMBO J. 2006 Nov 15;25(22):5433-42. Epub 2006 Nov 2. PMID:17082766
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