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==Crystal structure of the 2 ADP-bound V1 complex== | ==Crystal structure of the 2 ADP-bound V1 complex== | ||
<StructureSection load='5knb' size='340' side='right' caption='[[5knb]], [[Resolution|resolution]] 3.25Å' scene=''> | <StructureSection load='5knb' size='340' side='right'caption='[[5knb]], [[Resolution|resolution]] 3.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5knb]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KNB OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5knb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_hirae_ATCC_9790 Enterococcus hirae ATCC 9790]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KNB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.251Å</td></tr> | ||
<tr id=' | <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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5knb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5knb OCA], [https://pdbe.org/5knb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5knb RCSB], [https://www.ebi.ac.uk/pdbsum/5knb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5knb ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/NTPA_ENTHA NTPA_ENTHA] Involved in ATP-driven sodium extrusion. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
V1-ATPases are highly conserved ATP-driven rotary molecular motors found in various membrane systems. We recently reported the crystal structures for the Enterococcus hirae A3B3DF (V1) complex, corresponding to the catalytic dwell state waiting for ATP hydrolysis. Here we present the crystal structures for two other dwell states obtained by soaking nucleotide-free V1 crystals in ADP. In the presence of 20 muM ADP, two ADP molecules bind to two of three binding sites and cooperatively induce conformational changes of the third site to an ATP-binding mode, corresponding to the ATP-binding dwell. In the presence of 2 mM ADP, all nucleotide-binding sites are occupied by ADP to induce conformational changes corresponding to the ADP-release dwell. Based on these and previous findings, we propose a V1-ATPase rotational mechanism model. | |||
Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor.,Suzuki K, Mizutani K, Maruyama S, Shimono K, Imai FL, Muneyuki E, Kakinuma Y, Ishizuka-Katsura Y, Shirouzu M, Yokoyama S, Yamato I, Murata T Nat Commun. 2016 Oct 27;7:13235. doi: 10.1038/ncomms13235. PMID:27807367<ref>PMID:27807367</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5knb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Enterococcus hirae ATCC 9790]] | ||
[[Category: Imai | [[Category: Large Structures]] | ||
[[Category: Ishizuka-Katsura | [[Category: Imai FL]] | ||
[[Category: Kakinuma | [[Category: Ishizuka-Katsura Y]] | ||
[[Category: Maruyama | [[Category: Kakinuma Y]] | ||
[[Category: Mizutani | [[Category: Maruyama S]] | ||
[[Category: Muneyuki | [[Category: Mizutani K]] | ||
[[Category: Murata | [[Category: Muneyuki E]] | ||
[[Category: Shimono | [[Category: Murata T]] | ||
[[Category: Shirouzu | [[Category: Shimono K]] | ||
[[Category: Suzuki | [[Category: Shirouzu M]] | ||
[[Category: Yamato | [[Category: Suzuki K]] | ||
[[Category: Yokoyama | [[Category: Yamato I]] | ||
[[Category: Yokoyama S]] | |||
Latest revision as of 13:49, 27 September 2023
Crystal structure of the 2 ADP-bound V1 complexCrystal structure of the 2 ADP-bound V1 complex
Structural highlights
FunctionNTPA_ENTHA Involved in ATP-driven sodium extrusion. Publication Abstract from PubMedV1-ATPases are highly conserved ATP-driven rotary molecular motors found in various membrane systems. We recently reported the crystal structures for the Enterococcus hirae A3B3DF (V1) complex, corresponding to the catalytic dwell state waiting for ATP hydrolysis. Here we present the crystal structures for two other dwell states obtained by soaking nucleotide-free V1 crystals in ADP. In the presence of 20 muM ADP, two ADP molecules bind to two of three binding sites and cooperatively induce conformational changes of the third site to an ATP-binding mode, corresponding to the ATP-binding dwell. In the presence of 2 mM ADP, all nucleotide-binding sites are occupied by ADP to induce conformational changes corresponding to the ADP-release dwell. Based on these and previous findings, we propose a V1-ATPase rotational mechanism model. Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor.,Suzuki K, Mizutani K, Maruyama S, Shimono K, Imai FL, Muneyuki E, Kakinuma Y, Ishizuka-Katsura Y, Shirouzu M, Yokoyama S, Yamato I, Murata T Nat Commun. 2016 Oct 27;7:13235. doi: 10.1038/ncomms13235. PMID:27807367[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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