3gqb
From Proteopedia
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==Crystal Structure of the A3B3 complex from V-ATPase== | ==Crystal Structure of the A3B3 complex from V-ATPase== | ||
- | <StructureSection load='3gqb' size='340' side='right' caption='[[3gqb]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3gqb' size='340' side='right'caption='[[3gqb]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3gqb]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3gqb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GQB FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gqb OCA], [https://pdbe.org/3gqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gqb RCSB], [https://www.ebi.ac.uk/pdbsum/3gqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gqb ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/VATA_THET8 VATA_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/3gqb_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/3gqb_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
- | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3gqb ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Vacuolar-type ATPases (V-ATPases) exist in various cellular membranes of many organisms to regulate physiological processes by controlling the acidic environment. Here, we have determined the crystal structure of the A(3)B(3) subcomplex of V-ATPase at 2.8 A resolution. The overall construction of the A(3)B(3) subcomplex is significantly different from that of the alpha(3)beta(3) sub-domain in F(o)F(1)-ATP synthase, because of the presence of a protruding 'bulge' domain feature in the catalytic A subunits. The A(3)B(3) subcomplex structure provides the first molecular insight at the catalytic and non-catalytic interfaces, which was not possible in the structures of the separate subunits alone. Specifically, in the non-catalytic interface, the B subunit seems to be incapable of binding ATP, which is a marked difference from the situation indicated by the structure of the F(o)F(1)-ATP synthase. In the catalytic interface, our mutational analysis, on the basis of the A(3)B(3) structure, has highlighted the presence of a cluster composed of key hydrophobic residues, which are essential for ATP hydrolysis by V-ATPases. | ||
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- | Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilus.,Maher MJ, Akimoto S, Iwata M, Nagata K, Hori Y, Yoshida M, Yokoyama S, Iwata S, Yokoyama K EMBO J. 2009 Dec 2;28(23):3771-9. Epub 2009 Nov 5. PMID:19893485<ref>PMID:19893485</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
==See Also== | ==See Also== | ||
- | *[[ATPase|ATPase]] | + | *[[ATPase 3D structures|ATPase 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Thermus thermophilus | + | [[Category: Large Structures]] |
- | [[Category: Akimoto | + | [[Category: Thermus thermophilus HB8]] |
- | [[Category: Hori | + | [[Category: Akimoto S]] |
- | [[Category: Iwata | + | [[Category: Hori Y]] |
- | [[Category: Iwata | + | [[Category: Iwata M]] |
- | [[Category: Meher | + | [[Category: Iwata S]] |
- | [[Category: Nagata | + | [[Category: Meher M]] |
- | [[Category: Yokoyama | + | [[Category: Nagata K]] |
- | [[Category: Yokoyama | + | [[Category: Yokoyama K]] |
- | [[Category: Yoshida | + | [[Category: Yokoyama S]] |
- | + | [[Category: Yoshida M]] | |
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Current revision
Crystal Structure of the A3B3 complex from V-ATPase
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Categories: Large Structures | Thermus thermophilus HB8 | Akimoto S | Hori Y | Iwata M | Iwata S | Meher M | Nagata K | Yokoyama K | Yokoyama S | Yoshida M