7lgu

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Current revision (19:37, 29 May 2024) (edit) (undo)
 
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<StructureSection load='7lgu' size='340' side='right'caption='[[7lgu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='7lgu' size='340' side='right'caption='[[7lgu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7lgu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGU FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C14:TETRADECANE'>C14</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=HP6:HEPTANE'>HP6</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLC26A5, PRES ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C14:TETRADECANE'>C14</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=HP6:HEPTANE'>HP6</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</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=7lgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgu OCA], [https://pdbe.org/7lgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgu RCSB], [https://www.ebi.ac.uk/pdbsum/7lgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgu 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=7lgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgu OCA], [https://pdbe.org/7lgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgu RCSB], [https://www.ebi.ac.uk/pdbsum/7lgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgu ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[https://www.uniprot.org/uniprot/S26A5_HUMAN S26A5_HUMAN]] Autosomal recessive non-syndromic sensorineural deafness type DFNB. The disease is caused by variants affecting the gene represented in this entry.
 
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== Function ==
 
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[[https://www.uniprot.org/uniprot/S26A5_HUMAN S26A5_HUMAN]] Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity).
 
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
<div class="pdbe-citations 7lgu" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7lgu" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Prestin|Prestin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ge, J]]
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[[Category: Ge J]]
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[[Category: Gouaux, E]]
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[[Category: Gouaux E]]
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[[Category: Lipid interaction]]
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[[Category: Membrane protein]]
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[[Category: Transporter family]]
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Current revision

Structure of human prestin in the presence of NaCl

PDB ID 7lgu

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OCA

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