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1un7
From Proteopedia
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[[Category: n-acetyleglucosamine-6-phosphate]] | [[Category: n-acetyleglucosamine-6-phosphate]] | ||
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Revision as of 14:01, 30 October 2007
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THE 3-D STRUCTURE OF THE N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE, NAGA, FROM BACILLUS SUBTILIS: A MEMBER OF THE UREASE SUPERFAMILY
Overview
The enzyme N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes, the hydrolysis of the N-acetyl group of GlcNAc-6-P to yield glucosamine, 6-phosphate and acetate, the first committed step in the biosynthetic, pathway to amino-sugar-nucleotides. It is classified into carbohydrate, esterase family CE-9 (see afmb.cnrs-mrs.fr/CAZY/). Here we report the, cloning, expression, and three-dimensional structure (Protein Data Bank, code 1un7) determination by x-ray crystallography of the Bacillus subtilis, NagA at a resolution of 2.0 A. The structure presents two domains, a, (beta/alpha)(8) barrel enclosing the active center and a small beta barrel, domain. The structure is dimeric, and the substrate phosphate coordination, at the active center is provided by an Arg/His pair contributed from ... [(full description)]
About this Structure
1UN7 is a [Single protein] structure of sequence from [Bacillus subtilis] with GLP, FE and 2PE as [ligands]. Active as [N-acetylglucosamine-6-phosphate deacetylase], with EC number [3.5.1.25]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily., Vincent F, Yates D, Garman E, Davies GJ, Brannigan JA, J Biol Chem. 2004 Jan 23;279(4):2809-16. Epub 2003 Oct 13. PMID:14557261
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