4ryo
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MPG:1-MONOOLEOYL-RAC-GLYCEROL'>MPG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MPG:1-MONOOLEOYL-RAC-GLYCEROL'>MPG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ryi|4ryi]], [[4ryj|4ryj]], [[4rym|4rym]], [[4ryn|4ryn]], [[4ryq|4ryq]], [[4ryr|4ryr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ryi|4ryi]], [[4ryj|4ryj]], [[4rym|4rym]], [[4ryn|4ryn]], [[4ryq|4ryq]], [[4ryr|4ryr]]</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=4ryo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ryo RCSB], [http://www.ebi.ac.uk/pdbsum/4ryo PDBsum]</span></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=4ryo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryo OCA], [http://pdbe.org/4ryo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ryo RCSB], [http://www.ebi.ac.uk/pdbsum/4ryo PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Translocator proteins (TSPOs) bind steroids and porphyrins, and they are implicated in many human diseases, for which they serve as biomarkers and therapeutic targets. TSPOs have tryptophan-rich sequences that are highly conserved from bacteria to mammals. Here we report crystal structures for Bacillus cereus TSPO (BcTSPO) down to 1.7 A resolution, including a complex with the benzodiazepine-like inhibitor PK11195. We also describe BcTSPO-mediated protoporphyrin IX (PpIX) reactions, including catalytic degradation to a previously undescribed heme derivative. We used structure-inspired mutations to investigate reaction mechanisms, and we showed that TSPOs from Xenopus and man have similar PpIX-directed activities. Although TSPOs have been regarded as transporters, the catalytic activity in PpIX degradation suggests physiological importance for TSPOs in protection against oxidative stress. | ||
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| + | Protein structure. Structure and activity of tryptophan-rich TSPO proteins.,Guo Y, Kalathur RC, Liu Q, Kloss B, Bruni R, Ginter C, Kloppmann E, Rost B, Hendrickson WA Science. 2015 Jan 30;347(6221):551-5. doi: 10.1126/science.aaa1534. PMID:25635100<ref>PMID:25635100</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4ryo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 21:44, 15 October 2015
Crystal structure of BcTSPO type II high resolution monomer
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