Journal article

Structural insights into GDP-mediated regulation of a bacterial acyl-CoA thioesterase.

Yogesh B Khandokar, Parul Srivastava, Nathan Cowieson, Subir Sarker, David Aragao, Shubagata Das, Kate M Smith, Shane R Raidal, Jade K Forwood

Journal of Biological Chemistry | American Society for Biochemistry & Molecular Biology (ASBMB) | Published : 2017


Thioesterases catalyze the cleavage of thioester bonds within many activated fatty acids and acyl-CoA substrates. They are expressed ubiquitously in both prokaryotes and eukaryotes and are subdivided into 25 thioesterase families according to their catalytic active site, protein oligomerization, and substrate specificity. Although many of these enzyme families are well-characterized in terms of function and substrate specificity, regulation across most thioesterase families is poorly understood. Here, we characterized a TE6 thioesterase from the bacterium Neisseria meningitidis Structural analysis with X-ray crystallographic diffraction data to 2.0-Å revealed that each protein subunit harbor..

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