1w17
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(New page: 200px<br /><applet load="1w17" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w17, resolution 1.90Å" /> '''STRUCTURE OF BACILLU...)
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Revision as of 03:04, 21 November 2007
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STRUCTURE OF BACILLUS SUBTILIS PDAA, 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 acid and three histidines, all conserved in, the NodB homology domain, with the ligand. The PdaA structure provides a, template for interpreting the wealth of sequence data on family 4, carbohydrate esterases in a structural context and represents a first step, towards understanding the reaction mechanism of this family of enzymes.
About this Structure
1W17 is a Single protein structure of sequence from Bacillus subtilis. 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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