CATH Classification

Domain Context

CATH Clusters

Superfamily P-loop containing nucleotide triphosphate hydrolases
Functional Family ATP synthase subunit beta

Enzyme Information

7.1.2.2
H(+)-transporting two-sector ATPase.
based on mapping to UniProt Q6CFT7
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2).
-!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. -!- All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. -!- Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. -!- This movement is driven by the H(+) electrochemical potential gradient. -!- The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14.

UniProtKB Entries (1)

Q6C326
ATPA_YARLI
Yarrowia lipolytica CLIB122
ATP synthase subunit alpha, mitochondrial

PDB Structure

PDB 5FL7
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.
Hahn, A., Parey, K., Bublitz, M., Mills, D.J., Zickermann, V., Vonck, J., Kuhlbrandt, W., Meier, T.
Mol.Cell