5ezb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5ezb' size='340' side='right'caption='[[5ezb]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='5ezb' size='340' side='right'caption='[[5ezb]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ezb]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ezb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EZB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5ezb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ezb OCA], [https://pdbe.org/5ezb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ezb RCSB], [https://www.ebi.ac.uk/pdbsum/5ezb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ezb ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0FKN5_CHICK A0FKN5_CHICK] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 25: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Battistutta | [[Category: Battistutta R]] | ||
[[Category: Bonetto | [[Category: Bonetto G]] | ||
[[Category: Costanzi | [[Category: Costanzi E]] | ||
[[Category: Lolli | [[Category: Lolli G]] | ||
[[Category: Pasqualetto | [[Category: Pasqualetto E]] | ||
Latest revision as of 11:35, 12 July 2023
Chicken prestin STAS domainChicken prestin STAS domain
Structural highlights
FunctionPublication Abstract from PubMedPrestin is a unique ATP- and Ca2+-independent molecular motor with piezoelectric characteristic responsible for the electromotile properties of mammalian cochlear outer hair cells, that is the capacity of these cells to modify their length in response to electric stimuli. This "electromotility" is at the basis of the exceptional sensitivity and frequency selectivity distinctive of mammals. Prestin belongs to the SLC26 family of anion transporters and needs anions to function properly, in particular chloride. By X-ray crystallography here we reveal that the STAS domain of mammalian prestin, considered an "incomplete" transporter, harbor an unanticipated anion-binding site. In parallel we present the first crystal structure of a prestin STAS domain from a non-mammalian vertebrate prestin (chicken) that behaves as a "full" transporter. Notably, in chicken STAS the anion-binding site is lacking due to a local structural rearrangement, indicating that the presence of the STAS anion-binding site is exclusive to mammalian prestin. The STAS domain of mammalian SLC26A5 prestin harbors an anion-binding site.,Lolli G, Pasqualetto E, Costanzi E, Bonetto G, Battistutta R Biochem J. 2015 Dec 3. pii: BJ20151089. PMID:26635354[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||