1w1a
From Proteopedia
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Revision as of 14:16, 30 October 2007
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STRUCTURE OF BACILLUS SUBTILIS PDAA IN COMPLEX WITH NAG, A FAMILY 4 CARBOHYDRATE ESTERASE.
Overview
Family 4 carbohydrate esterases deacetylate polymeric carbohydrate, substrates such as chitin, acetyl xylan and peptidoglycan. Although some, of these enzymes have recently been enzymologically characterised, neither, their structure nor their reaction mechanism has been defined. Sequence, conservation in this family has pointed to a conserved core, termed the, NodB homology domain. We describe the cloning, purification and 1.9 A, crystal structure of PdaA, a peptidoglycan deacetylase from Bacillus, subtilis. The enzyme assumes a fold related to a (beta/alpha)8 barrel, with a long groove on the surface of the protein that harbours all, conserved residues. A complex with the substrate analogue, N-acetyl-glucosamine was refined to 2.25 A resolution, revealing, interactions of an aspartic ... [(full description)]
About this Structure
1W1A is a [Single protein] structure of sequence from [Bacillus subtilis] with NDG, CD and GOL as [ligands]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
Reference
Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine., Blair DE, van Aalten DM, FEBS Lett. 2004 Jul 16;570(1-3):13-9. PMID:15251431
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