|
|
| Line 3: |
Line 3: |
| | <SX load='6qum' size='340' side='right' viewer='molstar' caption='[[6qum]], [[Resolution|resolution]] 3.25Å' scene=''> | | <SX load='6qum' size='340' side='right' viewer='molstar' caption='[[6qum]], [[Resolution|resolution]] 3.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qum]] 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=6QUM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QUM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qum]] is a 26 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=6QUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QUM 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6r10|6r10]], [[6r0z|6r0z]], [[6r0y|6r0y]], [[6r0w|6r0w]]</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=6qum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qum OCA], [https://pdbe.org/6qum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qum RCSB], [https://www.ebi.ac.uk/pdbsum/6qum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qum ProSAT]</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=6qum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qum OCA], [http://pdbe.org/6qum PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qum RCSB], [http://www.ebi.ac.uk/pdbsum/6qum PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qum ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [https://www.uniprot.org/uniprot/VATD_THET8 VATD_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 28: |
Line 27: |
| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet8]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Sazanov, L]] | + | [[Category: Sazanov L]] |
| - | [[Category: Zhou, L]] | + | [[Category: Zhou L]] |
| - | [[Category: Atp hydrolysis/synthesis]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Proton translocation]]
| + | |
| - | [[Category: Rotary catalysis]]
| + | |
| Structural highlights
Function
VATD_THET8 Produces ATP from ADP in the presence of a proton gradient across the membrane.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhou L, Sazanov LA. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science. 2019 Aug 23;365(6455). pii: 365/6455/eaaw9144. doi:, 10.1126/science.aaw9144. PMID:31439765 doi:http://dx.doi.org/10.1126/science.aaw9144
|
