1gx3
From Proteopedia
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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, conservation among eubacterial NATs is restricted to structural residues, of the protein core, as well as the active site and a hinge that connects, the first two domains of the NAT structure. The structure of M. smegmatis, NAT provides a template for modelling the structure of the M. tuberculosis, enzyme and for structure-based ligand design as an approach to designing, anti-TB drugs.
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 Known structural/functional Site: . 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
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