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| | ==Crystal structure of native translocator protein 18kDa (TSPO) from Rhodobacter sphaeroides (A139T Mutant) in C2 space group== | | ==Crystal structure of native translocator protein 18kDa (TSPO) from Rhodobacter sphaeroides (A139T Mutant) in C2 space group== |
| - | <StructureSection load='5duo' size='340' side='right' caption='[[5duo]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='5duo' size='340' side='right'caption='[[5duo]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5duo]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DUO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5duo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DUO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PP9:PROTOPORPHYRIN+IX'>PP9</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uc1|4uc1]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PP9:PROTOPORPHYRIN+IX'>PP9</scene></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=5duo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5duo OCA], [http://pdbe.org/5duo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5duo RCSB], [http://www.ebi.ac.uk/pdbsum/5duo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5duo 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=5duo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5duo OCA], [https://pdbe.org/5duo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5duo RCSB], [https://www.ebi.ac.uk/pdbsum/5duo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5duo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TSPO_RHOSH TSPO_RHOSH]] May play a role in the transmembrane transport of tetrapyrroles and similar compounds, and thereby contribute to the regulation of tetrapyrrole biosynthesis (PubMed:10409680). Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX (PubMed:23651039). Binds protoporphyrin IX, hemin, and coproporphyrin III, but does not bind delta-aminolevulinic acid (PubMed:23952237, PubMed:20541505, PubMed:25635101). Can bind bilirubin, curcumin, gossypol, retinoic acid, cholesterol and the benzodiazepine receptor agonist PK-11195 (in vitro) (PubMed:23952237, PubMed:25635101). Plays a role in the response to low oxygen levels and in the regulation of the biosynthesis of photosynthetic pigments (PubMed:7673149, PubMed:10409680, PubMed:10681549).<ref>PMID:10681549</ref> <ref>PMID:20541505</ref> <ref>PMID:23651039</ref> <ref>PMID:23952237</ref> <ref>PMID:25635101</ref> <ref>PMID:7673149</ref> <ref>PMID:10409680</ref> | + | [https://www.uniprot.org/uniprot/TSPO_CERSP TSPO_CERSP] May play a role in the transmembrane transport of tetrapyrroles and similar compounds, and thereby contribute to the regulation of tetrapyrrole biosynthesis (PubMed:10409680). Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX (PubMed:23651039). Binds protoporphyrin IX, hemin, and coproporphyrin III, but does not bind delta-aminolevulinic acid (PubMed:23952237, PubMed:20541505, PubMed:25635101). Can bind bilirubin, curcumin, gossypol, retinoic acid, cholesterol and the benzodiazepine receptor agonist PK-11195 (in vitro) (PubMed:23952237, PubMed:25635101). Plays a role in the response to low oxygen levels and in the regulation of the biosynthesis of photosynthetic pigments (PubMed:7673149, PubMed:10409680, PubMed:10681549).<ref>PMID:10681549</ref> <ref>PMID:20541505</ref> <ref>PMID:23651039</ref> <ref>PMID:23952237</ref> <ref>PMID:25635101</ref> <ref>PMID:7673149</ref> <ref>PMID:10409680</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Wang comments that the diffraction data for the structure of the A139T mutant of translocator protein TSPO from Rhodobacter sphaeroides should be used to 1.65 instead of 1.8 angstroms and that the density interpreted as porphyrin and monoolein is better fitted as polyethylene glycol. Although different practices of data processing exist, in this case they do not substantially influence the final map. Additional data are presented supporting the fit of a porphyrin and monooleins.
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| - | | + | |
| - | Response to Comment on "Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism".,Li F, Liu J, Zheng Y, Garavito RM, Ferguson-Miller S Science. 2015 Oct 30;350(6260):519. doi: 10.1126/science.aab2595. Epub 2015 Oct, 29. PMID:26516277<ref>PMID:26516277</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5duo" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ferguson-Miller, S]] | + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: Garavito, R M]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, F]] | + | [[Category: Ferguson-Miller S]] |
| - | [[Category: Liu, J]] | + | [[Category: Garavito RM]] |
| - | [[Category: Zheng, Y]] | + | [[Category: Li F]] |
| - | [[Category: Transmembrane helice]] | + | [[Category: Liu J]] |
| - | [[Category: Membrane protein]] | + | [[Category: Zheng Y]] |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
TSPO_CERSP May play a role in the transmembrane transport of tetrapyrroles and similar compounds, and thereby contribute to the regulation of tetrapyrrole biosynthesis (PubMed:10409680). Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX (PubMed:23651039). Binds protoporphyrin IX, hemin, and coproporphyrin III, but does not bind delta-aminolevulinic acid (PubMed:23952237, PubMed:20541505, PubMed:25635101). Can bind bilirubin, curcumin, gossypol, retinoic acid, cholesterol and the benzodiazepine receptor agonist PK-11195 (in vitro) (PubMed:23952237, PubMed:25635101). Plays a role in the response to low oxygen levels and in the regulation of the biosynthesis of photosynthetic pigments (PubMed:7673149, PubMed:10409680, PubMed:10681549).[1] [2] [3] [4] [5] [6] [7]
References
- ↑ Yeliseev AA, Kaplan S. TspO of rhodobacter sphaeroides. A structural and functional model for the mammalian peripheral benzodiazepine receptor. J Biol Chem. 2000 Feb 25;275(8):5657-67. PMID:10681549
- ↑ Korkhov VM, Sachse C, Short JM, Tate CG. Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals. Structure. 2010 Jun 9;18(6):677-87. doi: 10.1016/j.str.2010.03.001. PMID:20541505 doi:http://dx.doi.org/10.1016/j.str.2010.03.001
- ↑ Ginter C, Kiburu I, Boudker O. Chemical catalysis by the translocator protein (18 kDa). Biochemistry. 2013 May 28;52(21):3609-11. doi: 10.1021/bi400364z. Epub 2013 May, 13. PMID:23651039 doi:http://dx.doi.org/10.1021/bi400364z
- ↑ Li F, Xia Y, Meiler J, Ferguson-Miller S. Characterization and modeling of the oligomeric state and ligand binding behavior of purified translocator protein 18 kDa from Rhodobacter sphaeroides. Biochemistry. 2013 Aug 27;52(34):5884-99. doi: 10.1021/bi400431t. Epub 2013 Aug, 16. PMID:23952237 doi:http://dx.doi.org/10.1021/bi400431t
- ↑ Li F, Liu J, Zheng Y, Garavito RM, Ferguson-Miller S. Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism. Science. 2015 Jan 30;347(6221):555-8. doi: 10.1126/science.1260590. PMID:25635101 doi:http://dx.doi.org/10.1126/science.1260590
- ↑ Yeliseev AA, Kaplan S. A sensory transducer homologous to the mammalian peripheral-type benzodiazepine receptor regulates photosynthetic membrane complex formation in Rhodobacter sphaeroides 2.4.1. J Biol Chem. 1995 Sep 8;270(36):21167-75. PMID:7673149
- ↑ Yeliseev AA, Kaplan S. A novel mechanism for the regulation of photosynthesis gene expression by the TspO outer membrane protein of Rhodobacter sphaeroides 2.4.1. J Biol Chem. 1999 Jul 23;274(30):21234-43. PMID:10409680
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