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Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation

Forwood, Jade; Thakur, Anil S.; Guncar, G; Marfori, Mary; Mouradov, Dmitri; Meng, Weining; Robinson, Jodie; Huber, Thomas; Kellie, Stuart; Martin, Jennifer Louise; Hume, D A; Kobe, Bostjan

Description

Acyl-CoA thioesterases (Acots) catalyze the hydrolysis of fatty acyl-CoA to free fatty acid and CoA and thereby regulate lipid metabolism and cellular signaling. We present a comprehensive structural and functional characterization of mouse acyl-CoA thioesterase 7 (Acot7). Whereas prokaryotic homologues possess a single thioesterase domain, mammalian Acot7 contains a pair of domains in tandem. We determined the crystal structures of both the N- and C-terminal domains of the mouse enzyme, and...[Show more]

CollectionsANU Research Publications
Date published: 2007
Type: Journal article
URI: http://hdl.handle.net/1885/61478
Source: PNAS - Proceedings of the National Academy of Sciences of the United States of America
DOI: 10.1073/pnas.0700974104

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