2c26

File:2c26.gif

spinqualitylabelsall models 2c26, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURAL BASIS FOR THE PROMISCUOUS SPECIFICITY OF THE CARBOHYDRATE-BINDING MODULES FROM THE BETA-SANDWICH SUPER FAMILY

OverviewOverview

Enzyme systems that attack the plant cell wall contain noncatalytic, carbohydrate-binding modules (CBMs) that mediate attachment to this, composite structure and play a pivotal role in maximizing the hydrolytic, process. Although xyloglucan, which includes a backbone of beta-1,4-glucan, decorated primarily with xylose residues, is a key component of the plant, cell wall, CBMs that bind to this polymer have not been identified. Here, we showed that the C-terminal domain of the modular Clostridium, thermocellum enzyme CtCel9D-Cel44A (formerly known as CelJ) comprises a, novel CBM (designated CBM44) that binds with equal affinity to cellulose, and xyloglucan. We also showed that accommodation of xyloglucan side, chains is a general feature of CBMs that bind to single cellulose chains., The ... [(full description)]

About this StructureAbout this Structure

2C26 is a [Single protein] structure of sequence from [Clostridium thermocellum] with CA and EDO as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains., Najmudin S, Guerreiro CI, Carvalho AL, Prates JA, Correia MA, Alves VD, Ferreira LM, Romao MJ, Gilbert HJ, Bolam DN, Fontes CM, J Biol Chem. 2006 Mar 31;281(13):8815-28. Epub 2005 Nov 28. PMID:16314409

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