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The structure and nucleotide occupancy of bovine mitochondrial F 1 ‐ATPase are not influenced by crystallisation at high concentrations of nucleotide
Author(s) -
Menz R.Ian,
Leslie Andrew G.W,
Walker John E
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02302-x
Subject(s) - nucleotide , atpase , protein subunit , crystallization , mutant , crystallography , biology , chemistry , escherichia coli , microbiology and biotechnology , biochemistry , enzyme , gene , organic chemistry
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 Å resolution with crystals grown in the presence of 5 mM AMPPNP and 5 μM ADP. Similar to previous structures of bovine F 1 ‐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.