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4ryi

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==Crystal structure of BcTSPO/PK11195 complex==
==Crystal structure of BcTSPO/PK11195 complex==
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<StructureSection load='4ryi' size='340' side='right' caption='[[4ryi]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
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<StructureSection load='4ryi' size='340' side='right'caption='[[4ryi]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ryi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RYI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ryi]] is a 2 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=4RYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PKA:N-[(2R)-BUTAN-2-YL]-1-(2-CHLOROPHENYL)-N-METHYLISOQUINOLINE-3-CARBOXAMIDE'>PKA</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">X-ray diffraction, [[Resolution|Resolution]] 3.49&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ryj|4ryj]], [[4rym|4rym]], [[4ryn|4ryn]], [[4ryo|4ryo]]</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=PKA:N-[(2R)-BUTAN-2-YL]-1-(2-CHLOROPHENYL)-N-METHYLISOQUINOLINE-3-CARBOXAMIDE'>PKA</scene></td></tr>
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<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=4ryi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryi OCA], [http://pdbe.org/4ryi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ryi RCSB], [http://www.ebi.ac.uk/pdbsum/4ryi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryi ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ryi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryi OCA], [https://pdbe.org/4ryi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ryi RCSB], [https://www.ebi.ac.uk/pdbsum/4ryi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryi ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ryi" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Guo, Y]]
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[[Category: Bacillus cereus ATCC 14579]]
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[[Category: Hendrickson, W A]]
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[[Category: Large Structures]]
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[[Category: Liu, Q]]
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[[Category: Guo Y]]
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[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]]
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[[Category: Hendrickson WA]]
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[[Category: Membrane protein]]
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[[Category: Liu Q]]
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[[Category: New york consortium on membrane protein structure]]
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[[Category: Nycomp]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Psi-biology]]
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[[Category: Receptor]]
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[[Category: Structural genomic]]
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Current revision

Crystal structure of BcTSPO/PK11195 complex

PDB ID 4ryi

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