V-ATPase
From Proteopedia
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| - | == Your Heading Here (maybe something like 'Structure') == | ||
| - | <StructureSection load='3j0j' size='350' side='right' caption='Fitted structure of Thermus thermophilus V-ATPase, based on the EMD-5335 (PDB entry [[3j0j]])' scene=''> | ||
| - | Anything in this section will appear adjacent to the 3D structure and will be scrollable. | ||
| - | |||
| - | <scene name='V-ATPase/Adp/1'>TextToBeDisplayed</scene> | ||
| - | </StructureSection> | ||
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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== | ||
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===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]] | [[1r5z]] | ||
| + | |||
| + | [[1u7l]] | ||
| + | |||
| + | [[1v9m]] | ||
| + | |||
| + | ====Subunit E==== | ||
| + | [[2kz9]] | ||
| + | |||
| + | [[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
Contents |
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
