4ryo
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ryo]] 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=4RYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYO FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ryo]] 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=4RYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYO FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MPG:[(Z)-OCTADEC-9-ENYL]+(2R)-2,3-BIS(OXIDANYL)PROPANOATE'>MPG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MPG:[(Z)-OCTADEC-9-ENYL]+(2R)-2,3-BIS(OXIDANYL)PROPANOATE'>MPG</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=4ryo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryo OCA], [https://pdbe.org/4ryo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ryo RCSB], [https://www.ebi.ac.uk/pdbsum/4ryo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryo 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=4ryo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryo OCA], [https://pdbe.org/4ryo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ryo RCSB], [https://www.ebi.ac.uk/pdbsum/4ryo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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> | [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. | ||
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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 == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of BcTSPO type II high resolution monomer
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