2v1o

From Proteopedia

Revision as of 15:37, 30 October 2007

CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF ACYL-COA THIOESTERASE 7

Overview

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, inferred the structure of the full-length enzyme using a combination of, chemical cross-linking, mass spectrometry, and molecular modeling. The, quaternary arrangement in Acot7 features a trimer of hotdog fold dimers., Both domains of Acot7 are required for activity, but only one of two, ... [(full description)]

About this Structure

2V1O is a [Single protein] structure of sequence from [Mus musculus] with COA as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation., Forwood JK, Thakur AS, Guncar G, Marfori M, Mouradov D, Meng W, Robinson J, Huber T, Kellie S, Martin JL, Hume DA, Kobe B, Proc Natl Acad Sci U S A. 2007 Jun 19;104(25):10382-7. Epub 2007 Jun 11. PMID:17563367

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