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2CC0

Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate

Summary for 2CC0
Entry DOI10.2210/pdb2cc0/pdb
DescriptorACETYL-XYLAN ESTERASE, ZINC ION, ACETATE ION, ... (4 entities in total)
Functional Keywordshydrolase, carbohydrate esterase
Biological sourceSTREPTOMYCES LIVIDANS
Total number of polymer chains2
Total formula weight41478.73
Authors
Primary citationTaylor, E.J.,Gloster, T.M.,Turkenburg, J.P.,Vincent, F.,Brzozowski, A.M.,Dupont, C.,Shareck, F.,Centeno, M.S.J.,Prates, J.A.M.,Puchart, V.,Ferreira, L.M.A.,Fontes, C.M.G.A.,Biely, P.,Davies, G.J.
Structure and Activity of Two Metal-Ion Dependent Acetyl Xylan Esterases Involved in Plant Cell Wall Degradation Reveals a Close Similarity to Peptidoglycan Deacetylases
J.Biol.Chem., 281:10968-, 2006
Cited by
PubMed Abstract: The enzymatic degradation of plant cell wall xylan requires the concerted action of a diverse enzymatic syndicate. Among these enzymes are xylan esterases, which hydrolyze the O-acetyl substituents, primarily at the O-2 position of the xylan backbone. All acetylxylan esterase structures described previously display a alpha/beta hydrolase fold with a "Ser-His-Asp" catalytic triad. Here we report the structures of two distinct acetylxylan esterases, those from Streptomyces lividans and Clostridium thermocellum, in native and complex forms, with x-ray data to between 1.6 and 1.0 A resolution. We show, using a novel linked assay system with PNP-2-O-acetylxyloside and a beta-xylosidase, that the enzymes are sugar-specific and metal ion-dependent and possess a single metal center with a chemical preference for Co2+. Asp and His side chains complete the catalytic machinery. Different metal ion preferences for the two enzymes may reflect the surprising diversity with which the metal ion coordinates residues and ligands in the active center environment of the S. lividans and C. thermocellum enzymes. These "CE4" esterases involved in plant cell wall degradation are shown to be closely related to the de-N-acetylases involved in chitin and peptidoglycan degradation (Blair, D. E., Schuettelkopf, A. W., MacRae, J. I., and Aalten, D. M. (2005) Proc. Natl. Acad. Sci. U. S. A., 102, 15429-15434), which form the NodB deacetylase "superfamily."
PubMed: 16431911
DOI: 10.1074/JBC.M513066200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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건을2024-11-06부터공개중

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