1h8h
From Proteopedia
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| , resolution 2.9Å | |||||||
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| Sites: | , , , , , , , , , , , and | ||||||
| Ligands: | , , , , | ||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 empty.
About this Structure
1H8H is a Protein complex structure of sequences from Bos taurus. 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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