V-ATPase: Difference between revisions
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==Introduction== | ==Introduction== | ||
V- | 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-ATPase components== | ==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 | 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.<ref>PMID:20450191</ref> | ||
==Mechanism of rotation== | ==Mechanism of rotation== | ||
| Line 16: | Line 10: | ||
===PDB=== | ===PDB=== | ||
[[3j0j]] | |||
====V1 complex==== | |||
[[3j0j]]: Fitted structure of Thermus Thermophilus in a 9.7Å resolution cryo-EM map. | |||
[[3a5c]] | [[3a5c]] | ||
[[3a5d]] | |||
====A3B3 complex==== | |||
[[3gqb]] | |||
====Subunit C==== | |||
[[1r5z]] | |||
[[1u7l]] | |||
[[1v9m]] | |||
====Subunit E==== | |||
[[2kz9]] | |||
[[3k5b]] | [[3k5b]] | ||
[[ | [[3v6i]] | ||
====Subunit F==== | |||
[[2d00]] | |||
====Subunit G==== | |||
[[2kwy]] | |||
[[2k88]] | |||
====Subunit H==== | |||
[[1ho8]] | |||
====Vo complex==== | |||
[[3aou]] | |||
[[2db4]] | |||
[[2bl2]] | |||
[[2cyd]] | |||
====Subunit a==== | |||
[[2rpw]] | |||
[[2nvj]] | |||
===EMDB=== | ===EMDB=== | ||
5335 | [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 /> | |||
Revision as of 12:20, 6 September 2012
Introduction
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 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 rotation
V-ATPase structures
PDB
V1 complex
3j0j: Fitted structure of Thermus Thermophilus in a 9.7Å resolution cryo-EM map.
A3B3 complex
Subunit C
Subunit E
Subunit F
Subunit G
Subunit H
Vo complex
Subunit a
EMDB
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.
References
- ↑ 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
