ATPase, V1/A1 complex, subunit E

ATPase, V1/A1 complex, subunit E(InterPro Protein Domain record)

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ATPase, V1/A1 complex, subunit E

InterPro Protein Domain record

description http://metadb.riken.jp/db/SciNetS_rib124i/prib124u1i

ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [<cite idref="PUB00020603"/>, <cite idref="PUB00020604"/>]. The different types include: <ul><li>F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).</li><li>V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.</li><li>A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases (though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases).</li><li>P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.</li><li>E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.</li> </ul> The V-ATPases (or V1V0-ATPase) and A-ATPases (or A1A0-ATPase) are each composed of two linked complexes: the V1 or A1 complex contains the catalytic core that hydrolyses/synthesizes ATP, and the V0 or A0 complex that forms the membrane-spanning pore. The V- and A-ATPases both contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [<cite idref="PUB00009752"/>, <cite idref="PUB00020609"/>, <cite idref="PUB00020618"/>]. The V- and A-ATPases more closely resemble one another in subunit structure than they do the F-ATPases, although the function of A-ATPases is closer to that of F-ATPases. This entry represents subunit E from the V1 and A1 complexes of V- and A-ATPases, respectively. Subunit E appears to form a tight interaction with subunit G in the F0 complex, which together may act as stators to prevent certain subunits from rotating with the central rotary element, much in the same way as the F0 complex subunit B does in F-ATPases [<cite idref="PUB00020636"/>]. In addition to its key role in stator structure, subunit E appears to have a role in mediating interactions with putative regulatory subunits [<cite idref="PUB00020637"/>]. More information about this protein can be found at Protein of the Month: ATP Synthases [<cite idref="PUB00020719"/>].

label http://www.w3.org/2000/01/rdf-schema#label