1gx3

From Proteopedia

Revision as of 13:17, 30 October 2007

M. SMEGMATIS ARYLAMINE N-ACETYL TRANSFERASE

Overview

Arylamine N-acetyltransferases which acetylate and inactivate isoniazid, an anti-tubercular drug, are found in mycobacteria including Mycobacterium, smegmatis and Mycobacterium tuberculosis. We have solved the structure of, arylamine N-acetyltransferase from M. smegmatis at a resolution of 1.7 A, as a model for the highly homologous NAT from M. tuberculosis. The fold, closely resembles that of NAT from Salmonella typhimurium, with a common, catalytic triad and domain structure that is similar to certain cysteine, proteases. The detailed geometry of the catalytic triad is typical of, enzymes which use primary alcohols or thiols as activated nucleophiles., Thermal mobility and structural variations identify parts of NAT which, might undergo conformational changes during catalysis. Sequence, ... [(full description)]

About this Structure

1GX3 is a [Single protein] structure of sequence from [Mycobacterium smegmatis]. Active as [Arylamine N-acetyltransferase], with EC number [2.3.1.5]. Structure known Active Site: TRA. Full crystallographic information is available from [OCA].

Reference

The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid., Sandy J, Mushtaq A, Kawamura A, Sinclair J, Sim E, Noble M, J Mol Biol. 2002 May 10;318(4):1071-83. PMID:12054803

Page seeded by OCA on Tue Oct 30 15:21:59 2007