CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.20 | Up-down Bundle | |
1.20.120 | Four Helix Bundle (Hemerythrin (Met), subunit A) | |
1.20.120.220 | ATP synthase, F0 complex, subunit A |
Domain Context
CATH Clusters
Superfamily | ATP synthase, F0 complex, subunit A |
Functional Family | ATP synthase subunit a |
Enzyme Information
3.6.3.14 |
H(+)-transporting two-sector ATPase.
based on mapping to UniProt P0AB98
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
-!- 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.
|
UniProtKB Entries (1)
P68699 |
ATPL_ECOLI
Escherichia coli K-12
ATP synthase subunit c
|
PDB Structure
PDB | 1C17 |
External Links | |
Method | SOLUTION NMR |
Organism | Escherichia |
Primary Citation |
Structural changes linked to proton translocation by subunit c of the ATP synthase.
Nature
|