2JDI
Ground state structure of F1-ATPase from bovine heart mitochondria (Bovine F1-ATPase crystallised in the absence of azide)
Summary for 2JDI
| Entry DOI | 10.2210/pdb2jdi/pdb |
| Related | 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1H8H 1NBM 1OHH 1QO1 1W0J 1W0K 2CK3 |
| Descriptor | ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, ATP SYNTHASE SUBUNIT BETA, ATP SYNTHASE GAMMA CHAIN, ... (8 entities in total) |
| Functional Keywords | atp phosphorylase, hydrolase, atp synthesis |
| Biological source | BOS TAURUS (BOVINE) More |
| Cellular location | Mitochondrion inner membrane (By similarity): P19483 Mitochondrion: P00829 P05631 P05630 P05632 |
| Total number of polymer chains | 9 |
| Total formula weight | 374867.90 |
| Authors | Bowler, M.W.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2007-01-09, release date: 2007-03-13, Last modification date: 2023-12-13) |
| Primary citation | Bowler, M.W.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. Ground State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 A Resolution J.Biol.Chem., 282:14238-, 2007 Cited by PubMed Abstract: The structure of bovine F(1)-ATPase, crystallized in the presence of AMP-PNP and ADP, but in the absence of azide, has been determined at 1.9A resolution. This structure has been compared with the previously described structure of bovine F(1)-ATPase determined at 1.95A resolution with crystals grown under the same conditions but in the presence of azide. The two structures are extremely similar, but they differ in the nucleotides that are bound to the catalytic site in the beta(DP)-subunit. In the present structure, the nucleotide binding sites in the beta(DP)- and beta(TP)-subunits are both occupied by AMP-PNP, whereas in the earlier structure, the beta(TP) site was occupied by AMP-PNP and the beta(DP) site by ADP, where its binding is enhanced by a bound azide ion. Also, the conformation of the side chain of the catalytically important residue, alphaArg-373 differs in the beta(DP)- and beta(TP)-subunits. Thus, the structure with bound azide represents the ADP inhibited state of the enzyme, and the new structure represents a ground state intermediate in the active catalytic cycle of ATP hydrolysis. PubMed: 17350959DOI: 10.1074/JBC.M700203200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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