V-ATPase

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-	[[3j0j]]: Fitted structure of Thermus Thermophilus in a 9.7Å resolution cryo-EM map.	+	[[3j0j]]: Fitted structure of Thermus thermophilus in a 9.7Å resolution cryo-EM map.
	[[3a5c]]		[[3a5c]]

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Revision as of 14:15, 6 September 2012

Contents 1 Introduction 2 V-ATPase components 2.1 V1-domain 2.2 V0-domain 3 Mechanism of rotation 4 V-ATPase structures 4.1 PDB 4.1.1 V1 complex 4.1.2 A3B3 complex 4.1.3 Subunit C 4.1.4 Subunit E 4.1.5 Subunit F 4.1.6 Subunit G 4.1.7 Subunit H 4.1.8 Vo complex 4.1.9 Subunit a 4.2 EMDB 5 References

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-ATPases are structurally and mechanically related to F- and A-ATPases.^[2]

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.^[3]

ATP hydrolysis occurs at catalytic sites located at the interface of the A and B subunits.

V1-domain

spinqualitylabelsall models V1-domain of V-ATPase of Thermus Thermophilus (PDB entry 3j0j) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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-domain

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. ↑ 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
3. ↑ 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