1w1b
|
STRUCTURE OF BACILLUS SUBTILIS PDAA WITH CADMIUM, A FAMILY 4 CARBOHYDRATE ESTERASE.
OverviewOverview
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 StructureAbout this Structure
1W1B is a Single protein structure of sequence from Bacillus subtilis with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Feb 3 10:18:01 2008