5FKR

Unraveling the first step of xyloglucan degradation by the soil saprophyte Cellvibrio japonicus through the functional and structural characterization of a potent GH74 endo-xyloglucanase

5FKR の概要

• エントリーDOI: 10.2210/pdb5fkr/pdb
• 関連するPDBエントリー: 5FKQ 5FKS 5FKT
• 分子名称: ENDO-1,4-BETA-GLUCANASE/XYLOGLUCANASE, PUTATIVE, GLY74A, BROMIDE ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, cellvibrio japonicus, xyloglucan saccharification, glycoside hydrolase, carbohydrate binding module, green fluorescent protein
• 由来する生物種: CELLVIBRIO JAPONICUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 78465.14

構造登録者

Attia, M.,Stepper, J.,Davies, G.J.,Brumer, H. (登録日: 2015-10-19, 公開日: 2015-11-25, 最終更新日: 2024-01-10)

主引用文献

Attia, M.,Stepper, J.,Davies, G.J.,Brumer, H.
Functional and Structural Characterization of a Potent Gh74 Endo-Xyloglucanase from the Soil Saprophyte Cellvibrio Japonicus Unravels the First Step of Xyloglucan Degradation.
FEBS J., 283:1701-, 2016

PubMed Abstract: The heteropolysaccharide xyloglucan (XyG) comprises up to one-quarter of the total carbohydrate content of terrestrial plant cell walls and, as such, represents a significant reservoir in the global carbon cycle. The complex composition of XyG requires a consortium of backbone-cleaving endo-xyloglucanases and side-chain cleaving exo-glycosidases for complete saccharification. The biochemical basis for XyG utilization by the model Gram-negative soil saprophytic bacterium Cellvibrio japonicus is incompletely understood, despite the recent characterization of associated side-chain cleaving exo-glycosidases. We present a detailed functional and structural characterization of a multimodular enzyme encoded by gene locus CJA_2477. The CJA_2477 gene product comprises an N-terminal glycoside hydrolase family 74 (GH74) endo-xyloglucanase module in train with two carbohydrate-binding modules (CBMs) from families 10 and 2 (CBM10 and CBM2). The GH74 catalytic domain generates Glc4 -based xylogluco-oligosaccharide (XyGO) substrates for downstream enzymes through an endo-dissociative mode of action. X-ray crystallography of the GH74 module, alone and in complex with XyGO products spanning the entire active site, revealed a broad substrate-binding cleft specifically adapted to XyG recognition, which is composed of two seven-bladed propeller domains characteristic of the GH74 family. The appended CBM10 and CBM2 members notably did not bind XyG, nor other soluble polysaccharides, and instead were specific cellulose-binding modules. Taken together, these data shed light on the first step of xyloglucan utilization by C. japonicus and expand the repertoire of GHs and CBMs for selective biomass analysis and utilization.

PubMed: 26929175
DOI: 10.1111/FEBS.13696

実験手法

X-RAY DIFFRACTION (2.28 Å)