V-ATPase
IntroductionIntroduction
Vacuolar (H+)-ATPases (V-ATPases)[1] are mainly found in vacuoles of eukaryotic cells where they catalyze the hydrolysis of ATP in order to transport solutes.
V-ATPase componentsV-ATPase components
The structure of the whole V-ATPase complex can be divided in two domains. The V1 domain, which consist of eight different sub-units (A-H) and is responsible for the hydrolysis of ATP, and the intermembrane V0 domain consisting of six different sub-units and which transports the protons.[2]
Mechanism of rotationMechanism of rotation
V-ATPase structuresV-ATPase structures
PDBPDB
V1 complexV1 complex
3j0j: Fitted structure of Thermus Thermophilus in a 9.7Å resolution cryo-EM map.
A3B3 complexA3B3 complex
Subunit CSubunit C
Subunit ESubunit E
Subunit FSubunit F
Subunit GSubunit G
Subunit HSubunit H
Vo complexVo complex
Subunit aSubunit a
EMDBEMDB
5335: 9.7Å resolution map of Thermus Thermophilus V-ATPase.
1888: 16Å resolution map of Thermus Thermophilus V-ATPase.
1640: 25Å resolution map of Saccharomyces cerevisiae V-ATPase.
1590: 17Å resolution map of Manduca sexta V-ATPase.
ReferencesReferences
- ↑ Forgac M. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat Rev Mol Cell Biol. 2007 Nov;8(11):917-29. PMID:17912264 doi:10.1038/nrm2272
- ↑ Toei M, Saum R, Forgac M. Regulation and isoform function of the V-ATPases. Biochemistry. 2010 Jun 15;49(23):4715-23. PMID:20450191 doi:10.1021/bi100397s