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2d00
From Proteopedia
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==Subunit F of V-type ATPase/synthase== | ==Subunit F of V-type ATPase/synthase== | ||
| - | <StructureSection load='2d00' size='340' side='right' caption='[[2d00]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='2d00' size='340' side='right'caption='[[2d00]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2d00]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2d00]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D00 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]] 2.2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d00 OCA], [https://pdbe.org/2d00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d00 RCSB], [https://www.ebi.ac.uk/pdbsum/2d00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d00 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/VATF_THET8 VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. |
== 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/d0/2d00_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d0/2d00_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=2d00 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 A resolution. The subunit reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli chemotaxis response regulator CheY. The structure was successfully placed into the low-resolution EM structure of the prokaryotic holo-V-ATPase at a location indicated by the results of crosslinking experiments. The crystal structure, together with the single-molecule analysis using fluorescence resonance energy transfer, showed that the subunit F exhibits two conformations, a 'retracted' form in the absence and an 'extended' form in the presence of ATP. Our results postulated that the subunit F is a regulatory subunit in the V-ATPase. | ||
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| - | Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus.,Makyio H, Iino R, Ikeda C, Imamura H, Tamakoshi M, Iwata M, Stock D, Bernal RA, Carpenter EP, Yoshida M, Yokoyama K, Iwata S EMBO J. 2005 Nov 16;24(22):3974-83. Epub 2005 Nov 10. PMID:16281059<ref>PMID:16281059</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2d00" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[ATPase|ATPase]] | + | *[[ATPase 3D structures|ATPase 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Bernal | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Carpenter | + | [[Category: Bernal RA]] |
| - | [[Category: Iino | + | [[Category: Carpenter EP]] |
| - | [[Category: Ikeda | + | [[Category: Iino R]] |
| - | [[Category: Imamura | + | [[Category: Ikeda C]] |
| - | [[Category: Iwata | + | [[Category: Imamura H]] |
| - | [[Category: Iwata | + | [[Category: Iwata M]] |
| - | [[Category: Makyio | + | [[Category: Iwata S]] |
| - | [[Category: Stock | + | [[Category: Makyio H]] |
| - | [[Category: Tamakoshi | + | [[Category: Stock D]] |
| - | [[Category: Yokoyama | + | [[Category: Tamakoshi M]] |
| - | [[Category: Yoshida | + | [[Category: Yokoyama K]] |
| - | + | [[Category: Yoshida M]] | |
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Current revision
Subunit F of V-type ATPase/synthase
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Categories: Large Structures | Thermus thermophilus | Bernal RA | Carpenter EP | Iino R | Ikeda C | Imamura H | Iwata M | Iwata S | Makyio H | Stock D | Tamakoshi M | Yokoyama K | Yoshida M

