5FUI

Crystal structure of the C-terminal CBM6 of LamC a marine laminarianse from Zobellia galactanivorans

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5FUI の概要

• エントリーDOI: 10.2210/pdb5fui/pdb
• 分子名称: ENDO-1,3-BETA-GLUCANASE, FAMILY GH16, GLYCEROL, 2-AMINOMETHYL-PYRIDINE, ... (5 entities in total)
• 機能のキーワード: hydrolase, carbohydrate binding module, cbm6, polysaccharide fixation, marine bacterial laminarinase, zobellia galactanivorans
• 由来する生物種: ZOBELLIA GALACTANIVORANS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14845.38

構造登録者

Labourel, A.,Jam, M.,Legentil, L.,Sylla, B.,Hehemann, J.H.,Ficko-Blean, E.,Ferrieres, V.,Czjzek, M.,Michel, G. (登録日: 2016-01-27, 公開日: 2016-03-02, 最終更新日: 2024-01-10)

主引用文献

Jam, M.,Ficko-Blean, E.,Labourel, A.,Larocque, R.,Czjzek, M.,Michel, G.
Unraveling the Multivalent Binding of a Marine Family 6 Carbohydrate-Binding Module with its Native Laminarin Ligand.
FEBS J., 283:1863-, 2016

PubMed Abstract: Laminarin is an abundant brown algal storage polysaccharide. Marine microorganisms, such as Zobellia galactanivorans, produce laminarinases for its degradation, which are important for the processing of this organic matter in the ocean carbon cycle. These laminarinases are often modular, as is the case with ZgLamC which has an N-terminal GH16 module, a central family 6 carbohydrate-binding module (CBM) and a C-terminal PorSS module. To date, no studies have characterized a true marine laminarin-binding CBM6 with its natural carbohydrate ligand. The crystal structure of ZgLamCCBM6 indicates that this CBM has two clefts for binding sugar (variable loop site, VLS; and concave face site, CFS). The ZgLamCCBM6 VLS binds in an exo-manner and the CFS interacts in an endo-manner with laminarin. Isothermal titration calorimetry (ITC) experiments on native and mutant ZgLamCCBM6 confirm that these binding sites have different modes of recognition for laminarin, in agreement with the 'regional model' postulated for CBM6-binding modules. Based on ITC data and structural data, we propose a model of ZgLamCCBM6 interacting with different chains of laminarin in a multivalent manner, forming a complex cross-linked protein-polysaccharide network.

PubMed: 26959085
DOI: 10.1111/FEBS.13707

実験手法

X-RAY DIFFRACTION (1.4 Å)