4RYN
Crystal structure of BcTSPO, type1 monomer
Summary for 4RYN
| Entry DOI | 10.2210/pdb4ryn/pdb |
| Related | 4RYI 4RYJ 4RYM 4RYO |
| Descriptor | Integral membrane protein, [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate, DODECYL-ALPHA-D-MALTOSIDE, ... (6 entities in total) |
| Functional Keywords | structural genomics, psi-biology, protein structure initiative, new york consortium on membrane protein structure, nycomps, receptor, membrane protein |
| Biological source | Bacillus cereus |
| Cellular location | Cell membrane ; Multi-pass membrane protein : Q81BL7 |
| Total number of polymer chains | 1 |
| Total formula weight | 25503.60 |
| Authors | Guo, Y.,Liu, Q.,Hendrickson, W.A.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2014-12-15, release date: 2015-02-11, Last modification date: 2023-09-20) |
| Primary citation | Guo, Y.,Kalathur, R.C.,Liu, Q.,Kloss, B.,Bruni, R.,Ginter, C.,Kloppmann, E.,Rost, B.,Hendrickson, W.A. Protein structure. Structure and activity of tryptophan-rich TSPO proteins. Science, 347:551-555, 2015 Cited by PubMed Abstract: 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 Å 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. PubMed: 25635100DOI: 10.1126/science.aaa1534 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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