1H8H
Bovine mitochondrial F1-ATPase crystallised in the presence of 5mm AMPPNP
Summary for 1H8H
Entry DOI | 10.2210/pdb1h8h/pdb |
Related | 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1NBM 1QO1 |
Descriptor | BOVINE MITOCHONDRIAL F1-ATPASE, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (9 entities in total) |
Functional Keywords | atp phosphorylase, atp phosphorylase (h+ transporting), atp synthase, f1fo atp synthase, f1-atpase, hydrolase |
Biological source | BOS TAURUS (CATTLE) More |
Cellular location | Mitochondrion inner membrane : P19483 Mitochondrion: P00829 P05631 |
Total number of polymer chains | 7 |
Total formula weight | 354127.32 |
Authors | Braig, K.,Menz, R.I.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2001-02-06, release date: 2001-04-15, Last modification date: 2023-12-13) |
Primary citation | Menz, R.I.,Leslie, A.G.W.,Walker, J.E. The Structure and Nucleotide Occupancy of Bovine Mitochondrial F(1)-ATPase are not Influenced by Crystallisation at High Concentrations of Nucleotide FEBS Lett., 494:11-, 2001 Cited by PubMed Abstract: Analysis of tryptophan mutants of F(1)-ATPase from Escherichia coli [Löbau et al. (1997) FEBS Lett. 404, 15-18] suggested that nucleotide concentrations used to grow crystals for the determination of the structure of bovine F(1)-ATPase [Abrahams et al. (1994) Nature 370, 621-628] would be sufficient to occupy only two catalytic sites, and that higher concentrations of nucleotide would result in all three sites being occupied. We have determined the structure of bovine F(1)-ATPase at 2.9 A resolution with crystals grown in the presence of 5 mM AMPPNP and 5 microM ADP. Similar to previous structures of bovine F(1)-ATPase determined with crystals grown in the presence of lower nucleotide concentrations, only two beta-subunits have bound nucleotide and the third subunit remains empty. PubMed: 11297725DOI: 10.1016/S0014-5793(01)02302-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
