2JEP

Native family 5 xyloglucanase from Paenibacillus pabuli

2JEP の概要

• エントリーDOI: 10.2210/pdb2jep/pdb
• 関連するPDBエントリー: 2JEP
• 分子名称: XYLOGLUCANASE, 1,2-ETHANEDIOL, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: family 5, xyloglucanase, plant cell wall, hydrolase
• 由来する生物種: PAENIBACILLUS PABULI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88206.10

構造登録者

Gloster, T.M.,Ibatullin, F.M.,Macauley, K.,Eklof, J.M.,Roberts, S.,Turkenburg, J.P.,Bjornvad, M.E.,Jorgensen, P.L.,Danielsen, S.,Johansen, K.,Borchert, T.V.,Wilson, K.S.,Brumer, H.,Davies, G.J. (登録日: 2007-01-18, 公開日: 2007-03-20, 最終更新日: 2023-12-13)

主引用文献

Gloster, T.M.,Ibatullin, F.M.,Macauley, K.,Eklof, J.M.,Roberts, S.,Turkenburg, J.P.,Bjornvad, M.E.,Jorgensen, P.L.,Danielsen, S.,Johansen, K.,Borchert, T.V.,Wilson, K.S.,Brumer, H.,Davies, G.J.
Characterization and Three-Dimensional Structures of Two Distinct Bacterial Xyloglucanases from Families Gh5 and Gh12.
J.Biol.Chem., 282:19177-, 2007

PubMed Abstract: The plant cell wall is a complex material in which the cellulose microfibrils are embedded within a mesh of other polysaccharides, some of which are loosely termed "hemicellulose." One such hemicellulose is xyloglucan, which displays a beta-1,4-linked d-glucose backbone substituted with xylose, galactose, and occasionally fucose moieties. Both xyloglucan and the enzymes responsible for its modification and degradation are finding increasing prominence, reflecting both the drive for enzymatic biomass conversion, their role in detergent applications, and the utility of modified xyloglucans for cellulose fiber modification. Here we present the enzymatic characterization and three-dimensional structures in ligand-free and xyloglucan-oligosaccharide complexed forms of two distinct xyloglucanases from glycoside hydrolase families GH5 and GH12. The enzymes, Paenibacillus pabuli XG5 and Bacillus licheniformis XG12, both display open active center grooves grafted upon their respective (beta/alpha)(8) and beta-jelly roll folds, in which the side chain decorations of xyloglucan may be accommodated. For the beta-jelly roll enzyme topology of GH12, binding of xylosyl and pendant galactosyl moieties is tolerated, but the enzyme is similarly competent in the degradation of unbranched glucans. In the case of the (beta/alpha)(8) GH5 enzyme, kinetically productive interactions are made with both xylose and galactose substituents, as reflected in both a high specific activity on xyloglucan and the kinetics of a series of aryl glycosides. The differential strategies for the accommodation of the side chains of xyloglucan presumably facilitate the action of these microbial hydrolases in milieus where diverse and differently substituted substrates may be encountered.

PubMed: 17376777
DOI: 10.1074/JBC.M700224200

実験手法

X-RAY DIFFRACTION (1.4 Å)