3a5c

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{{STRUCTURE_3a5c| PDB=3a5c | SCENE= }}
 
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===Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase===
 
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{{ABSTRACT_PUBMED_19779483}}
 
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==About this Structure==
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==Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase==
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[[3a5c]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5C OCA].
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<StructureSection load='3a5c' size='340' side='right'caption='[[3a5c]], [[Resolution|resolution]] 4.51&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3a5c]] is a 16 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=3A5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A5C FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.51&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5c OCA], [https://pdbe.org/3a5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a5c RCSB], [https://www.ebi.ac.uk/pdbsum/3a5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/3a5c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3a5c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation scheme, architecture and subunit composition. However, there is no detailed structural information on V-ATPases despite the abundant biochemical and biophysical research. Here, we report a crystallographic study of V1-ATPase, from Thermus thermophilus, which is a soluble component consisting of A, B, D and F subunits. The structure at 4.5 A resolution reveals inter-subunit interactions and nucleotide binding. In particular, the structure of the central stalk composed of D and F subunits was shown to be characteristic of V1-ATPases. Small conformational changes of respective subunits and significant rearrangement of the quaternary structure observed in the three AB pairs were related to the interaction with the straight central stalk. The rotation mechanism is discussed based on a structural comparison between V1-ATPases and F1-ATPases.
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==See Also==
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Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase.,Numoto N, Hasegawa Y, Takeda K, Miki K EMBO Rep. 2009 Nov;10(11):1228-34. Epub 2009 Sep 25. PMID:19779483<ref>PMID:19779483</ref>
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*[[ATP synthase|ATP synthase]]
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*[[V-ATPase|V-ATPase]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:019779483</ref><references group="xtra"/>
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</div>
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[[Category: Thermus thermophilus]]
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<div class="pdbe-citations 3a5c" style="background-color:#fffaf0;"></div>
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[[Category: Hasegawa, Y.]]
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[[Category: Miki, K.]]
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==See Also==
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[[Category: Numoto, N.]]
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*[[ATPase 3D structures|ATPase 3D structures]]
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[[Category: Takeda, K.]]
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== References ==
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[[Category: Asymmetric]]
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<references/>
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[[Category: Atp synthesis]]
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__TOC__
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[[Category: Atp-binding]]
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</StructureSection>
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[[Category: Hydrogen ion transport]]
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[[Category: Large Structures]]
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[[Category: Hydrolase]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Ion transport]]
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[[Category: Hasegawa Y]]
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[[Category: Nucleotide-binding]]
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[[Category: Miki K]]
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[[Category: Rotation]]
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[[Category: Numoto N]]
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[[Category: Transport]]
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[[Category: Takeda K]]
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[[Category: V-atpase]]
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[[Category: Vacuolar type]]
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Current revision

Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase

PDB ID 3a5c

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