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{{STRUCTURE_3j0j|  PDB=3j0j  |  SCENE=  }}
===Fitted atomic models of Thermus thermophilus V-ATPase subunits into cryo-EM map===
{{ABSTRACT_PUBMED_22178924}}


==Function==
==Fitted atomic models of Thermus thermophilus V-ATPase subunits into cryo-EM map==
[[http://www.uniprot.org/uniprot/VATE_THET8 VATE_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/VATF_THET8 VATF_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://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. [[http://www.uniprot.org/uniprot/VATD_THET8 VATD_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/VATC_THET8 VATC_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/VATB_THET8 VATB_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.  
<SX load='3j0j' size='340' side='right' viewer='molstar' caption='[[3j0j]], [[Resolution|resolution]] 9.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3j0j]] is a 13 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=3J0J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J0J FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.7&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0j OCA], [https://pdbe.org/3j0j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j0j RCSB], [https://www.ebi.ac.uk/pdbsum/3j0j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0j ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ion-translocating rotary ATPases serve either as ATP synthases, using energy from a transmembrane ion motive force to create the cell's supply of ATP, or as transmembrane ion pumps that are powered by ATP hydrolysis. The members of this family of enzymes each contain two rotary motors: one that couples ion translocation to rotation and one that couples rotation to ATP synthesis or hydrolysis. During ATP synthesis, ion translocation through the membrane-bound region of the complex causes rotation of a central rotor that drives conformational changes and ATP synthesis in the catalytic region of the complex. There are no structural models available for the intact membrane region of any ion-translocating rotary ATPase. Here we present a 9.7 A resolution map of the H(+)-driven ATP synthase from Thermus thermophilus obtained by electron cryomicroscopy of single particles in ice. The 600-kilodalton complex has an overall subunit composition of A(3)B(3)CDE(2)FG(2)IL(12). The membrane-bound motor consists of a ring of L subunits and the carboxy-terminal region of subunit I, which are equivalent to the c and a subunits of most other rotary ATPases, respectively. The map shows that the ring contains 12 L subunits and that the I subunit has eight transmembrane helices. The L(12) ring and I subunit have a surprisingly small contact area in the middle of the membrane, with helices from the I subunit making contacts with two different L subunits. The transmembrane helices of subunit I form bundles that could serve as half-channels across the membrane, with the first half-channel conducting protons from the periplasm to the L(12) ring and the second half-channel conducting protons from the L(12) ring to the cytoplasm. This structure therefore suggests the mechanism by which a transmembrane proton motive force is converted to rotation in rotary ATPases.


==About this Structure==
Subnanometre-resolution structure of the intact Thermus thermophilus H(+)-driven ATP synthase.,Lau WC, Rubinstein JL Nature. 2011 Dec 18. doi: 10.1038/nature10699. PMID:22178924<ref>PMID:22178924</ref>
[[3j0j]] is a 13 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=3J0J OCA].
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3j0j" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ATP synthase|ATP synthase]]
*[[ATPase 3D structures|ATPase 3D structures]]
*[[V-ATPase|V-ATPase]]
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:022178924</ref><references group="xtra"/><references/>
</SX>
[[Category: Thermus thermophilus]]
[[Category: Large Structures]]
[[Category: Lau, W C.Y.]]
[[Category: Thermus thermophilus HB8]]
[[Category: Rubinstein, J L.]]
[[Category: Lau WCY]]
[[Category: Flexible fitting]]
[[Category: Rubinstein JL]]
[[Category: Hydrolase]]
[[Category: Membrane protein complex]]
[[Category: Rigid body fitting]]
Retrieved from "https://proteopedia.org/3j0j"