7v75
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Thermostabilized human prestin in complex with salicylate== | ==Thermostabilized human prestin in complex with salicylate== | ||
| - | <StructureSection load='7v75' size='340' side='right'caption='[[7v75]], [[Resolution|resolution]] 3. | + | <StructureSection load='7v75' size='340' side='right'caption='[[7v75]], [[Resolution|resolution]] 3.57Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7v75]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V75 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7v75]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V75 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=LBN:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine'>LBN</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</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]] 3.57Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=LBN:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine'>LBN</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</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=7v75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v75 OCA], [https://pdbe.org/7v75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v75 RCSB], [https://www.ebi.ac.uk/pdbsum/7v75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v75 ProSAT]</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=7v75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v75 OCA], [https://pdbe.org/7v75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v75 RCSB], [https://www.ebi.ac.uk/pdbsum/7v75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v75 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Outer hair cell elecromotility, driven by prestin, is essential for mammalian cochlear amplification. Here, we report the cryo-EM structures of thermostabilized prestin (Pres(TS)), complexed with chloride, sulfate, or salicylate at 3.52-3.63 A resolutions. The central positively-charged cavity allows flexible binding of various anion species, which likely accounts for the known distinct modulations of nonlinear capacitance (NLC) by different anions. Comparisons of these Pres(TS) structures with recent prestin structures suggest rigid-body movement between the core and gate domains, and provide mechanistic insights into prestin inhibition by salicylate. Mutations at the dimeric interface severely diminished NLC, suggesting that stabilization of the gate domain facilitates core domain movement, thereby contributing to the expression of NLC. These findings advance our understanding of the molecular mechanism underlying mammalian cochlear amplification. | ||
| + | |||
| + | Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.,Futamata H, Fukuda M, Umeda R, Yamashita K, Tomita A, Takahashi S, Shikakura T, Hayashi S, Kusakizako T, Nishizawa T, Homma K, Nureki O Nat Commun. 2022 Oct 20;13(1):6208. doi: 10.1038/s41467-022-34017-x. PMID:36266333<ref>PMID:36266333</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7v75" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Prestin|Prestin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Thermostabilized human prestin in complex with salicylate
| |||||||||||
