1odt

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1odt, resolution 1.70Å

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CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH ACETATE

Overview

Esterases and deacetylases active on carbohydrate ligands have been, classified into 14 families based upon amino acid sequence similarities., Enzymes from carbohydrate esterase family seven (CE-7) are unusual in that, they display activity towards both acetylated xylooligosaccharides and the, antibiotic, cephalosporin C. The 1.9A structure of the multifunctional, CE-7 esterase (hereinafter CAH) from Bacillus subtilis 168 reveals a, classical alpha/beta hydrolase fold encased within a 32 hexamer. This is, the first example of a hexameric alpha/beta hydrolase and is further, evidence of the versatility of this particular fold, which is used in a, wide variety of biological contexts. A narrow entrance tunnel leads to the, centre of the molecule, where the six active-centre catalytic triads ... [(full description)]

About this Structure

1ODT is a [Single protein] structure of sequence from [Bacillus subtilis] with ACT as [ligand]. Active as [[1]], with EC number [3.1.1.41]. Full crystallographic information is available from [OCA].

Reference

Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution., Vincent F, Charnock SJ, Verschueren KH, Turkenburg JP, Scott DJ, Offen WA, Roberts S, Pell G, Gilbert HJ, Davies GJ, Brannigan JA, J Mol Biol. 2003 Jul 11;330(3):593-606. PMID:12842474

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