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2CC0

Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate

2CC0 の概要
エントリーDOI10.2210/pdb2cc0/pdb
分子名称ACETYL-XYLAN ESTERASE, ZINC ION, ACETATE ION, ... (4 entities in total)
機能のキーワードhydrolase, carbohydrate esterase
由来する生物種STREPTOMYCES LIVIDANS
タンパク質・核酸の鎖数2
化学式量合計41478.73
構造登録者
主引用文献Taylor, 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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 2cc0
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

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