title: Crystallization of the acyl-CoA thioesterase TesB from Yersinia pestis.
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.
authors: School of Biomedical Sciences, Charles Sturt University, Boorooma Street, Wagga Wagga, NSW 2678, Australia.
authors: Crystall M D
authors: CM
authors: Swarbrick
authors: Edward I
authors: EI
authors: Patterson
authors: Jade K
authors: JK
authors: Forwood
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D012995:Solubility; D013869:Thiolester Hydrolases / Q000737:chemistry*; D015010:Yersinia pestis / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D013869:Thiolester Hydrolases
keywords: TesB; Yersinia pestis; hotdog domain; thioesterase
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