View source for 8igw


==Hexameric Ring Complex of Engineered V1-ATPase bound to 4 ADPs: A3(De)3_(ADP)3cat,1non-cat, Hexameric Ring Complex of Engineered V1-ATPase bound to 5 ADPs: A3(De)3_(ADP)3cat,2non-cat==
<StructureSection load='8igw' size='340' side='right'caption='[[8igw]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8igw]] is a 12 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=8IGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IGW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.2&#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>, <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=8igw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8igw OCA], [https://pdbe.org/8igw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8igw RCSB], [https://www.ebi.ac.uk/pdbsum/8igw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8igw ProSAT]</span></td></tr>
</table>
== 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 ==
Allostery produces concerted functions of protein complexes by orchestrating the cooperative work between the constituent subunits. Here we describe an approach to create artificial allosteric sites in protein complexes. Certain protein complexes contain subunits with pseudo-active sites, which are believed to have lost functions during evolution. Our hypothesis is that allosteric sites in such protein complexes can be created by restoring the lost functions of pseudo-active sites. We used computational design to restore the lost ATP-binding ability of the pseudo-active site in the B subunit of a rotary molecular motor, V(1)-ATPase. Single-molecule experiments with X-ray crystallography analyses revealed that binding of ATP to the designed allosteric site boosts this V(1)'s activity compared with the wild-type, and the rotation rate can be tuned by modulating ATP's binding affinity. Pseudo-active sites are widespread in nature, and our approach shows promise as a means of programming allosteric control over concerted functions of protein complexes.

Design of allosteric sites into rotary motor V(1)-ATPase by restoring lost function of pseudo-active sites.,Kosugi T, Iida T, Tanabe M, Iino R, Koga N Nat Chem. 2023 Nov;15(11):1591-1598. doi: 10.1038/s41557-023-01256-4. Epub 2023 , Jul 6. PMID:37414880<ref>PMID:37414880</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8igw" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterococcus hirae ATCC 9790]]
[[Category: Large Structures]]
[[Category: Koga N]]
[[Category: Kosugi T]]
[[Category: Tanabe M]]