Summary for 4QFW
| Entry DOI | 10.2210/pdb4qfw/pdb |
| Descriptor | Acyl-CoA thioesterase II (2 entities in total) |
| Functional Keywords | double-hotdog, 4hbt-like, thioesterase, acyl-coa thioesterase, hydrolase |
| Biological source | Yersinia pestis |
| Total number of polymer chains | 4 |
| Total formula weight | 130811.68 |
| Authors | Swarbrick, C.M.D.,Forwood, J.K. (deposition date: 2014-05-21, release date: 2014-06-04, Last modification date: 2023-09-20) |
| Primary citation | Swarbrick, C.M.,Patterson, E.I.,Forwood, J.K. Crystallization of the acyl-CoA thioesterase TesB from Yersinia pestis. Acta Crystallogr.,Sect.F, 69:188-190, 2013 Cited by PubMed Abstract: Yersinia pestis is a highly virulent human pathogen and is the causative agent of bubonic plague. Spread through the bite of infected fleas, plague epidemics have marked important events in history, including the Justinian plague (6th century), the Black Death (14th century) which decimated nearly one quarter of the European population, and more recently the Orientalis plague (1894). To date, deaths are still being reported and, without treatment, the disease kills most people within 4 days. One of the thioesterases from Y. pestis, TesB, is a broad-range acyl-CoA thioesterase and is highly conserved within prokaryotes and throughout evolution, sharing sequence similarity with the HIV Nef binding protein ACOT8. Here the expression, purification, crystallization and diffraction of TesB are reported. TesB has been recombinantly expressed and crystallized using the vapour-diffusion hanging-drop technique at pH 7.0 and 290 K. After optimization, crystals diffracted to 2.0 Å resolution at the Australian Synchrotron and belong to the space group P12(1)1 (a = 73.55, b = 170.82, c = 101.98 Å), with eight molecules likely to be present in the asymmetric unit. PubMed: 23385765DOI: 10.1107/S1744309113001267 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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