The structure and nucleotide occupancy of bovine mitochondrial F1‐ATPase are not influenced by crystallisation at high concentrations of nucleotide

FEBS Letters

Menz, R.Ian¹  Walker, John E¹  Leslie, Andrew G.W¹ 

[1] The Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH Cambridge, UK

关键词: Mitochondrion;    ATP synthase;    Catalytic site;    Nucleotide;    Crystal structure;    AMPPNP;    5′-adenylyl-imidodiphosphate;    rms;    root mean square;   

DOI  :  10.1016/S0014-5793(01)02302-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Analysis of tryptophan mutants of F₁-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 F₁-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 F₁-ATPase at 2.9 Å resolution with crystals grown in the presence of 5 mM AMPPNP and 5 μM ADP. Similar to previous structures of bovine F₁-ATPase determined with crystals grown in the presence of lower nucleotide concentrations, only two β-subunits have bound nucleotide and the third subunit remains empty.

【 授权许可】

Unknown