3PZT

Structure of the endo-1,4-beta-glucanase from Bacillus subtilis 168 with manganese(II) ion

Summary for 3PZT

• Entry DOI: 10.2210/pdb3pzt/pdb
• Related: 3PZU 3PZV
• Descriptor: Endoglucanase, MANGANESE (II) ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: alpha/beta barrel, glycosyl hydrolase, cellulose binding, hydrolase
• Biological source: Bacillus subtilis subsp. subtilis
• Total number of polymer chains: 2
• Total formula weight: 72777.54

Authors

Santos, C.R.,Paiva, J.H.,Akao, P.K.,Meza, A.N.,Silva, J.C.,Squina, F.M.,Ward, R.J.,Ruller, R.,Murakami, M.T. (deposition date: 2010-12-14, release date: 2011-09-14, Last modification date: 2024-02-21)

Primary citation

Santos, C.R.,Paiva, J.H.,Sforca, M.L.,Neves, J.L.,Navarro, R.Z.,Cota, J.,Akao, P.K.,Hoffmam, Z.B.,Meza, A.N.,Smetana, J.H.,Nogueira, M.L.,Polikarpov, I.,Xavier-Neto, J.,Squina, F.M.,Ward, R.J.,Ruller, R.,Zeri, A.C.,Murakami, M.T.
Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168.
Biochem.J., 441:95-104, 2012

PubMed Abstract: Cellulases participate in a number of biological events, such as plant cell wall remodelling, 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 by both their low catalytic efficiency and stability. In the present study, we conducted a detailed functional and structural characterization of the thermostable BsCel5A (Bacillus subtilis cellulase 5A), which consists of a GH5 (glycoside hydrolase 5) catalytic domain fused to a CBM3 (family 3 carbohydrate-binding module). 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 was 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.

PubMed: 21880019
DOI: 10.1042/BJ20110869

Experimental method

X-RAY DIFFRACTION (1.97 Å)