3a5c

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{{Seed}}
 
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[[Image:3a5c.png|left|200px]]
 
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==Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase==
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The line below this paragraph, containing "STRUCTURE_3a5c", creates the "Structure Box" on the page.
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<StructureSection load='3a5c' size='340' side='right'caption='[[3a5c]], [[Resolution|resolution]] 4.51&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_3a5c| PDB=3a5c | SCENE= }}
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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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===Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3a5c" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19779483}}, adds the Publication Abstract to the page
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*[[ATPase 3D structures|ATPase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19779483 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19779483}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3A5C is a 16 chains structure of sequences 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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[[Category: Thermus thermophilus HB8]]
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[[Category: Hasegawa Y]]
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==Reference==
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[[Category: Miki K]]
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<ref group="xtra">PMID:19779483</ref><references group="xtra"/>
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[[Category: Numoto N]]
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[[Category: Thermus thermophilus]]
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[[Category: Takeda K]]
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[[Category: Hasegawa, Y.]]
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[[Category: Miki, K.]]
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[[Category: Numoto, N.]]
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[[Category: Takeda, K.]]
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[[Category: Asymmetric]]
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[[Category: Atp synthesis]]
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[[Category: Atp-binding]]
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[[Category: Crystal structure]]
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[[Category: Hydrogen ion transport]]
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[[Category: Hydrolase]]
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[[Category: Ion transport]]
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[[Category: Nucleotide-binding]]
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[[Category: Rotation]]
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[[Category: Transport]]
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[[Category: V-atpase]]
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[[Category: Vacuolar type]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 18 17:48:45 2009''
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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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