V-ATPase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 59: Line 59:
[[2nvj]]
[[2nvj]]
- 
- 
- 
===EMDB===
===EMDB===

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.

3a5c

3a5d

A3B3 complex

3gqb

Subunit C

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

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

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Gydo van Zundert, Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/V-ATPase"
Personal tools