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| | <StructureSection load='4ryi' size='340' side='right'caption='[[4ryi]], [[Resolution|resolution]] 3.49Å' scene=''> | | <StructureSection load='4ryi' size='340' side='right'caption='[[4ryi]], [[Resolution|resolution]] 3.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ryi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. 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> | + | <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> |
| - | </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> | + | </td></tr><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> |
| - | <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>
| + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC_3136, DSM 31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</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=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> | + | |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baccr]] | + | [[Category: Bacillus cereus ATCC 14579]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guo, Y]] | + | [[Category: Guo Y]] |
| - | [[Category: Hendrickson, W A]] | + | [[Category: Hendrickson WA]] |
| - | [[Category: Liu, Q]] | + | [[Category: Liu Q]] |
| - | [[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]]
| + | |
| Structural highlights
Function
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][1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo Y, Kalathur RC, Liu Q, Kloss B, Bruni R, Ginter C, Kloppmann E, Rost B, Hendrickson WA. Protein structure. Structure and activity of tryptophan-rich TSPO proteins. Science. 2015 Jan 30;347(6221):551-5. doi: 10.1126/science.aaa1534. PMID:25635100 doi:http://dx.doi.org/10.1126/science.aaa1534
- ↑ Guo Y, Kalathur RC, Liu Q, Kloss B, Bruni R, Ginter C, Kloppmann E, Rost B, Hendrickson WA. Protein structure. Structure and activity of tryptophan-rich TSPO proteins. Science. 2015 Jan 30;347(6221):551-5. doi: 10.1126/science.aaa1534. PMID:25635100 doi:http://dx.doi.org/10.1126/science.aaa1534
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