5ezb
From Proteopedia
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| - | ''' | + | ==Chicken prestin STAS domain== |
| + | <StructureSection load='5ezb' size='340' side='right' caption='[[5ezb]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ezb]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EZB FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3llo|3llo]], [[5eus|5eus]], [[5euu|5euu]], [[5euw|5euw]], [[5eux|5eux]], [[5euz|5euz]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ezb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ezb OCA], [http://pdbe.org/5ezb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ezb RCSB], [http://www.ebi.ac.uk/pdbsum/5ezb PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Prestin 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 | + | 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<ref>PMID:26635354</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ezb" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Battistutta, R]] | ||
| + | [[Category: Bonetto, G]] | ||
| + | [[Category: Costanzi, E]] | ||
[[Category: Lolli, G]] | [[Category: Lolli, G]] | ||
[[Category: Pasqualetto, E]] | [[Category: Pasqualetto, E]] | ||
| - | [[Category: | + | [[Category: Eukaryotic slc26 stas fold]] |
| - | [[Category: | + | [[Category: Transport protein]] |
| - | + | ||
Revision as of 13:46, 16 December 2015
Chicken prestin STAS domain
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