|Title||The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide.|
|Publication Type||Journal Article|
|Year of Publication||2001|
|Authors||Menz, RI, Leslie, AG, Walker, JE|
|Date Published||2001 Apr 06|
|Keywords||Adenosine Diphosphate, Adenylyl Imidodiphosphate, Animals, Catalytic Domain, Cattle, Crystallization, Mitochondria, Models, Molecular, Nucleotides, Protein Structure, Secondary, Proton-Translocating ATPases|
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.
|Alternate Journal||FEBS Lett.|