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| | <StructureSection load='3a5c' size='340' side='right'caption='[[3a5c]], [[Resolution|resolution]] 4.51Å' scene=''> | | <StructureSection load='3a5c' size='340' side='right'caption='[[3a5c]], [[Resolution|resolution]] 4.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a5c]] is a 16 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=3A5C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A5C FirstGlance]. <br> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.51Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a5d|3a5d]]</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='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=3.6.3.14 3.6.3.14] </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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3a5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5c OCA], [http://pdbe.org/3a5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a5c RCSB], [http://www.ebi.ac.uk/pdbsum/3a5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thermus thermophilus]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Hasegawa, Y]] | + | [[Category: Hasegawa Y]] |
| - | [[Category: Miki, K]] | + | [[Category: Miki K]] |
| - | [[Category: Numoto, N]] | + | [[Category: Numoto N]] |
| - | [[Category: Takeda, K]] | + | [[Category: Takeda K]] |
| - | [[Category: Asymmetric]]
| + | |
| - | [[Category: Atp synthesis]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Hydrogen ion transport]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Rotation]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: V-atpase]]
| + | |
| - | [[Category: Vacuolar type]]
| + | |
| Structural highlights
Function
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.
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 PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Numoto N, Hasegawa Y, Takeda K, Miki K. Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase. EMBO Rep. 2009 Nov;10(11):1228-34. Epub 2009 Sep 25. PMID:19779483 doi:10.1038/embor.2009.202
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