Protein Family Models

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)

Date:

2024-10-16

This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella. [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)

Date:

2024-10-16

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)

Date:

2024-10-16

A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.

Date:

2024-05-30

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.

Gene:

atpD

Date:

2024-10-21