4rym: Difference between revisions
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==Crystal structure of BcTSPO Iodo Type1 monomer== | |||
<StructureSection load='4rym' size='340' side='right'caption='[[4rym]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4rym]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=4rym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rym OCA], [https://pdbe.org/4rym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rym RCSB], [https://www.ebi.ac.uk/pdbsum/4rym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rym ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TSPO_BACCR TSPO_BACCR] Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX (PubMed:25635100). Can bind the benzodiazepine receptor agonist PK-11195 (in vitro); this interferes with photooxidative tetrapyrrole degradation (PubMed:25635100). May play a role in the transmembrane transport of tetrapyrroles and similar compounds (By similarity).[UniProtKB:Q9RFC8]<ref>PMID:25635100</ref> | |||
<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> | |||
<div class="pdbe-citations 4rym" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus cereus ATCC 14579]] | |||
[[Category: Large Structures]] | |||
[[Category: Guo Y]] | |||
[[Category: Hendrickson WA]] | |||
[[Category: Liu Q]] | |||
