7tao: Difference between revisions

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-====
+==Cryo-EM structure of bafilomycin A1 bound to yeast VO V-ATPase==
-<StructureSection load='7tao' size='340' side='right'caption='[[7tao]]' scene=''>
+<StructureSection load='7tao' size='340' side='right'caption='[[7tao]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7tao]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TAO FirstGlance]. <br>
-</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=7tao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tao OCA], [https://pdbe.org/7tao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tao RCSB], [https://www.ebi.ac.uk/pdbsum/7tao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tao ProSAT]</span></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]] 3.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=WEV:(3~{Z},5~{E},7~{R},8~{S},9~{R},11~{E},13~{E},15~{S},16~{R})-3,15-dimethoxy-5,7,9,11-tetramethyl-16-[(2~{S},3~{R},4~{S})-4-[(2~{R},4~{R},5~{S},6~{R})-5-methyl-2,4-bis(oxidanyl)-6-propan-2-yl-oxan-2-yl]-3-oxidanyl-pentan-2-yl]-8-oxidanyl-1-oxacyclohexadeca-3,5,11,13-tetraen-2-one'>WEV</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=7tao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tao OCA], [https://pdbe.org/7tao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tao RCSB], [https://www.ebi.ac.uk/pdbsum/7tao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tao ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/VATL2_YEAST VATL2_YEAST] Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:1837023</ref> <ref>PMID:9030535</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Vacuolar-type adenosine triphosphatases (V-ATPases) are proton pumps found in almost all eukaryotic cells. These enzymes consist of a soluble catalytic V(1) region that hydrolyzes ATP and a membrane-embedded V(O) region responsible for proton translocation. V-ATPase activity leads to acidification of endosomes, phagosomes, lysosomes, secretory vesicles, and the trans-Golgi network, with extracellular acidification occurring in some specialized cells. Small-molecule inhibitors of V-ATPase have played a crucial role in elucidating numerous aspects of cell biology by blocking acidification of intracellular compartments, while therapeutic use of V-ATPase inhibitors has been proposed for the treatment of cancer, osteoporosis, and some infections. Here, we determine structures of the isolated V(O) complex from Saccharomyces cerevisiae bound to two well-known macrolide inhibitors: bafilomycin A1 and archazolid A. The structures reveal different binding sites for the inhibitors on the surface of the proton-carrying c ring, with only a small amount of overlap between the two sites. Binding of both inhibitors is mediated primarily through van der Waals interactions in shallow pockets and suggests that the inhibitors block rotation of the ring. Together, these structures indicate the existence of a large chemical space available for V-ATPase inhibitors that block acidification by binding the c ring.
+Cryo-EM of the Yeast V(O) Complex Reveals Distinct Binding Sites for Macrolide V-ATPase Inhibitors.,Keon KA, Benlekbir S, Kirsch SH, Muller R, Rubinstein JL ACS Chem Biol. 2022 Mar 18;17(3):619-628. doi: 10.1021/acschembio.1c00894. Epub , 2022 Feb 11. PMID:35148071<ref>PMID:35148071</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7tao" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Z-disk]]
+[[Category: Saccharomyces cerevisiae]]
+[[Category: Benlekbir S]]
+[[Category: Keon KA]]
+[[Category: Kirsch SH]]
+[[Category: Muller R]]
+[[Category: Rubinstein JL]]