4ryj
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of apo dimer of BcTSPO== |
+ | <StructureSection load='4ryj' size='340' side='right' caption='[[4ryj]], [[Resolution|resolution]] 4.10Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4ryj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RYJ FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ryi|4ryi]], [[4rym|4rym]], [[4ryn|4ryn]], [[4ryo|4ryo]]</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=4ryj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ryj RCSB], [http://www.ebi.ac.uk/pdbsum/4ryj PDBsum]</span></td></tr> | ||
+ | </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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Guo, Y]] | [[Category: Guo, Y]] | ||
+ | [[Category: Hendrickson, W A]] | ||
[[Category: Liu, Q]] | [[Category: Liu, Q]] | ||
- | [[Category: | + | [[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]] |
+ | [[Category: Membrane protein]] | ||
+ | [[Category: New york consortium on membrane protein structure]] | ||
+ | [[Category: Nycomp]] | ||
+ | [[Category: PSI, Protein structure initiative]] | ||
+ | [[Category: Psi-biology]] | ||
+ | [[Category: Receptor]] | ||
+ | [[Category: Structural genomic]] |
Revision as of 11:49, 12 February 2015
Crystal structure of apo dimer of BcTSPO
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