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==Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus== | |||
<StructureSection load='1v9m' size='340' side='right'caption='[[1v9m]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v9m]] is a 1 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=1V9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V9M FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | |||
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=1v9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9m OCA], [https://pdbe.org/1v9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v9m RCSB], [https://www.ebi.ac.uk/pdbsum/1v9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v9m ProSAT], [https://www.topsan.org/Proteins/RSGI/1v9m TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VATC_THET8 VATC_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/1v9m_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=1v9m ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft. | |||
Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution.,Numoto N, Kita A, Miki K Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:15103125<ref>PMID:15103125</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1v9m" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: | |||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Kita | [[Category: Kita A]] | ||
[[Category: Miki | [[Category: Miki K]] | ||
[[Category: Numoto | [[Category: Numoto N]] | ||
Latest revision as of 10:33, 30 October 2024
Crystal structure of the C subunit of V-type ATPase from Thermus thermophilusCrystal structure of the C subunit of V-type ATPase from Thermus thermophilus
Structural highlights
FunctionVATC_THET8 Produces ATP from ADP in the presence of a proton gradient across the membrane. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft. Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution.,Numoto N, Kita A, Miki K Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:15103125[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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