2l8a

Structure of a novel CBM3 lacking the calcium-binding site

spinqualitylabelsall models 2l8a, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l8a is a 1 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3pzu, 3pzv, 3pzt Gene: eglS, bglC, gld, BSU18130 (Bacillus subtilis) Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Cellulases participate in a number of biological events such as plant cell wall remodeling, nematode parasitism and microbial carbon uptake. Their ability to depolymerize crystalline cellulose is of great biotechnological interest for environmentally-compatible production of fuels from lignocellulosic biomass. However, industrial use of cellulases is somewhat limited both by their low catalytic efficiency and stability. In this work, we conducted a detailed functional and structural characterization of the thermostable cellulase 5A from Bacillus subtilis (BsCel5A), which consists of a GH5 catalytic domain fused to a family 3 carbohydrate-binding module (CBM3). NMR structural analysis revealed that the Bacillus CBM3 represents a new subfamily, which lacks the classical calcium-binding motif and variations in NMR frequencies in the presence of cellopentaose showed the importance of polar residues in the carbohydrate interaction. Together with the catalytic domain, the CBM3 forms a large planar surface for cellulose recognition, which conducts the substrate in a proper conformation to the active site and increases enzymatic efficiency. Notably, the manganese ion demonstrated to have a hyper-stabilizing effect on BsCel5A and by using deletion constructs and X-ray crystallography, we determined that this effect maps to a negatively charged motif located at the opposite face of the catalytic site. Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168.,Santos C, Paiva J, Sforca M, Neves J, Navarro R, Cota J, Akao P, Hoffmam ZB, Meza A, Smetana J, Nogueira M, Polikarpov I, Xavier-Neto J, Squina F, Ward RJ, Ruller R, Zeri A, Murakami MT Biochem J. 2011 Sep 1. PMID:21880019 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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