6r10
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Thermus thermophilus V/A-type ATPase/synthase, rotational state 1R== | |
| + | <SX load='6r10' size='340' side='right' viewer='molstar' caption='[[6r10]], [[Resolution|resolution]] 4.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6r10]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R10 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6R10 FirstGlance]. <br> | ||
| + | </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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qum|6qum]], [[6r0w|6r0w]], [[6r0z|6r0z]], [[6r0y|6r0y]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.1.2.2 7.1.2.2] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6r10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r10 OCA], [http://pdbe.org/6r10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r10 RCSB], [http://www.ebi.ac.uk/pdbsum/6r10 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r10 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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/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. [[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/VATF_THET8 VATF_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact Thermus thermophilus V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V1 and Vo in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V1-Vo torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family. | ||
| - | + | Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.,Zhou L, Sazanov LA Science. 2019 Aug 23;365(6455). pii: 365/6455/eaaw9144. doi:, 10.1126/science.aaw9144. PMID:31439765<ref>PMID:31439765</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6r10" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[ATPase 3D structures|ATPase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thet8]] | ||
| + | [[Category: Sazanov, L]] | ||
| + | [[Category: Zhou, L]] | ||
| + | [[Category: Atp hydrolysis/synthesis]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Proton translocation]] | ||
| + | [[Category: Rotary catalysis]] | ||
Current revision
Thermus thermophilus V/A-type ATPase/synthase, rotational state 1R
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