1h8h
From Proteopedia
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[[Category: f1fo atp synthase]] | [[Category: f1fo atp synthase]] | ||
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Revision as of 13:27, 30 October 2007
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BOVINE MITOCHONDRIAL F1-ATPASE CRYSTALLISED IN THE PRESENCE OF 5MM AMPPNP
Overview
Analysis of tryptophan mutants of F(1)-ATPase from Escherichia coli [Lobau, 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, ... [(full description)]
About this Structure
1H8H is a [Protein complex] structure of sequences from [Bos taurus] with MG, PO4, ATP, ADP and GOL as [ligands]. Active as [Transferred entry: 3.6.3.14], with EC number [3.6.1.34]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9, BC1, BC2, CAT and PLP. Full crystallographic information is available from [OCA].
Reference
The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide., Menz RI, Leslie AG, Walker JE, FEBS Lett. 2001 Apr 6;494(1-2):11-4. PMID:11297725
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