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C-terminal domain of V and A type ATP synthase
This entry represents a small alpha helical domain found at the C-terminus of a variety of ATP synthases. Paper describing PDB structure 1fx0. [1]. 11032839. The structure of the chloroplast F1-ATPase at 3.2 A resolution. Groth G, Pohl E;. J Biol Chem. 2001;276:1345-1352. Paper describing PDB structure 1mab. [2]. 9736690. The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis. Bianchet MA, Hullihen J, Pedersen PL, Amzel LM;. Proc Natl Acad Sci U S A. 1998;95:11065-11070. Paper describing PDB structure 1nbm. [3]. 9687365. Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism. Orriss GL, Leslie AG, Braig K, Walker JE;. Structure. 1998;6:831-837. (from Pfam)
ATP synthase alpha/beta family, nucleotide-binding domain
This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho. [1]. 8065448. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Abrahams JP, Leslie AG, Lutter R, Walker JE;. Nature 1994;370:621-628. [2]. 9261073. The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Shirakihara Y, Leslie AG, Abrahams JP, Walker JE, Ueda T, Sekimoto Y, Kambara M, Saika K, Kagawa Y, Yoshida M;. Structure 1997;5:825-836. (from Pfam)
F0F1 ATP synthase subunit beta
F0F1 ATP synthase subunit beta is part of the catalytic core of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane and is found in bacterial, mitochondrial, and chloroplast membranes
The F0F1 ATP synthase can produce ATP in the presence of a proton gradient across the membrane. Members of this family are the beta subunit of the F1 sector. The alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. Catalytic sites belong primarily to the beta-subunit.
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