V-ATPase: Difference between revisions
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== | ==Introduction== | ||
< | Vacuolar (H+)-ATPases (V-ATPases)<ref>PMID:17912264</ref> are mainly found in vacuoles of eukaryotic cells where they catalyze the hydrolysis of [[ATP]] in order to transport solutes. V-ATPases are structurally and mechanically related to F- and A-ATPases.<ref>PMID:15473999</ref> | ||
<scene name='V-ATPase/ | ==V-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 (a, d, e, c, c' and c") and which acts as a proton translocator from the cytoplasm to the lumen.<ref>PMID:20450191</ref> | |||
ATP hydrolysis occurs at catalytic sites located at the interface of the A and B subunits. | |||
===V1-domain=== | |||
<StructureSection load='3a5c' size='250' side='right' caption='V1-domain of V-ATPase of Thermus Thermophilus (PDB entry [[3j0j]])' scene='V-ATPase/V1-part/1'> | |||
The <scene name='V-ATPase/V1-part/1'>V1-domain</scene> consist of the A3B3 complex where the hydrolysis of ATP occurs (<scene name='V-ATPase/V1-part/3'>A is blue, B is red</scene>), subunit C (<scene name='V-ATPase/V1-part/8'>green</scene>), the D-subunit which is the central stalk (<scene name='V-ATPase/V1-part/2'>purple</scene>), subunit E (<scene name='V-ATPase/V1-part/6'>orange</scene>), subunit F (<scene name='V-ATPase/V1-part/4'>yellow</scene>)and subunit G (<scene name='V-ATPase/V1-part/7'>dark green</scene>). | |||
</StructureSection> | </StructureSection> | ||
== | ===V0-domain=== | ||
==Mechanism of rotation== | ==Mechanism of rotation== | ||
==V-ATPase structures== | ==3D V-ATPase structures== | ||
See [[ATPase]] | |||
[[ | |||
[ | ===EMDB=== | ||
[http://www.ebi.ac.uk/pdbe-srv/emsearch/atlas/5335_summary.html 5335]: 9.7Å resolution map of Thermus Thermophilus V-ATPase. | |||
[ | [http://www.ebi.ac.uk/pdbe-srv/emsearch/atlas/1888_summary.html 1888]: 16Å resolution map of Thermus Thermophilus V-ATPase. | ||
[ | [http://www.ebi.ac.uk/pdbe-srv/emsearch/atlas/1640_summary.html 1640]: 25Å resolution map of Saccharomyces cerevisiae V-ATPase. | ||
[http://www.ebi.ac.uk/pdbe-srv/emsearch/atlas/1590_summary.html 1590]: 17Å resolution map of Manduca sexta V-ATPase. | |||
==References== | ==References== | ||
<references /> | |||
Latest revision as of 13:55, 28 February 2016
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-ATPases are structurally and mechanically related to F- and A-ATPases.[2]
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 (a, d, e, c, c' and c") and which acts as a proton translocator from the cytoplasm to the lumen.[3]
ATP hydrolysis occurs at catalytic sites located at the interface of the A and B subunits.
V1-domainV1-domain
The consist of the A3B3 complex where the hydrolysis of ATP occurs (), subunit C (), the D-subunit which is the central stalk (), subunit E (), subunit F ()and subunit G (). |
| ||||||||||
V0-domainV0-domain
Mechanism of rotationMechanism of rotation
3D V-ATPase structures3D V-ATPase structures
See ATPase
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
- ↑ Cross RL, Muller V. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 2004 Oct 8;576(1-2):1-4. PMID:15473999 doi:10.1016/j.febslet.2004.08.065
- ↑ 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