Journal article

Structural and functional characterization of TesB from Yersinia pestis reveals a unique octameric arrangement of hotdog domains

CMD Swarbrick, MA Perugini, N Cowieson, JK Forwood

Acta crystallographica. Section D, Structural biology | INT UNION CRYSTALLOGRAPHY | Published : 2015

Abstract

Acyl-CoA thioesterases catalyse the hydrolysis of the thioester bonds present within a wide range of acyl-CoA substrates, releasing free CoASH and the corresponding fatty-acyl conjugate. The TesB-type thioesterases are members of the TE4 thioesterase family, one of 25 thioesterase enzyme families characterized to date, and contain two fused hotdog domains in both prokaryote and eukaryote homologues. Only two structures have been elucidated within this enzyme family, and much of the current understanding of the TesB thioesterases has been based on the Escherichia coli structure. Yersinia pestis, a highly virulent bacterium, encodes only one TesB-type thioesterase in its genome; here, the stru..

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University of Melbourne Researchers