1SKY
CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3
Summary for 1SKY
Entry DOI | 10.2210/pdb1sky/pdb |
Descriptor | F1-ATPASE, SULFATE ION (3 entities in total) |
Functional Keywords | atp synthase, f1fo atp synthase, f1-atpase, alpha3beta3 subcomplex of f1-atpase, hydrolase |
Biological source | Bacillus sp. More |
Cellular location | Cell membrane; Peripheral membrane protein (By similarity): P09219 P07677 |
Total number of polymer chains | 2 |
Total formula weight | 106838.54 |
Authors | Shirakihara, Y.,Leslie, A.G.W.,Abrahams, J.P.,Walker, J.E.,Ueda, T.,Sekimoto, Y.,Kambara, M.,Saika, K.,Kagawa, Y.,Yoshida, M. (deposition date: 1997-02-26, release date: 1998-03-04, Last modification date: 2024-02-14) |
Primary citation | Shirakihara, Y.,Leslie, A.G.,Abrahams, J.P.,Walker, J.E.,Ueda, T.,Sekimoto, Y.,Kambara, M.,Saika, K.,Kagawa, Y.,Yoshida, M. The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Structure, 5:825-836, 1997 Cited by PubMed Abstract: F1-ATPase, an oligomeric assembly with subunit stoichiometry alpha 3 beta 3 gamma delta epsilon, is the catalytic component of the ATP synthase complex, which plays a central role in energy transduction in bacteria, chloroplasts and mitochondria. The crystal structure of bovine mitochondrial F1-ATPase displays a marked asymmetry in the conformation and nucleotide content of the catalytic beta subunits. The alpha 3 beta 3 subcomplex of F1-ATPase has been assembled from subunits of the moderately thermophilic Bacillus PS3 made in Escherichia coli, and the subcomplex is active but does not show the catalytic cooperativity of intact F1-ATPase. The structure of this subcomplex should provide new information on the conformational variability of F1-ATPase and may provide insights into the unusual catalytic mechanism employed by this enzyme. PubMed: 9261073DOI: 10.1016/S0969-2126(97)00236-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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