4qp0 | pdb_00004qp0

Crystal Structure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei

spinqualitylabelsall models 4qp0, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qp0 is a 1 chain structure with sequence from Rhizomucor miehei. This structure supersedes the now removed PDB entry 4l3m. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L7SVX1_RHIMI Publication Abstract from PubMed beta-Mannosidases are exo-acting glycoside hydrolases (GHs) that catalyse the removal of the nonreducing end beta-D-mannose from manno-oligosaccharides or mannoside-substituted molecules. They play important roles in fundamental biological processes and also have potential applications in various industries. In this study, the first fungal GH family 5 beta-mannosidase (RmMan5B) from Rhizomucor miehei was functionally and structurally characterized. RmMan5B exhibited a much higher activity against manno-oligosaccharides than against p-nitrophenyl beta-D-mannopyranoside (pNPM) and had a transglycosylation activity which transferred mannosyl residues to sugars such as fructose. To investigate its substrate specificity and transglycosylation activity, crystal structures of RmMan5B and of its inactive E202A mutant in complex with mannobiose, mannotriose and mannosyl-fructose were determined at resolutions of 1.3, 2.6, 2.0 and 2.4 A, respectively. In addition, the crystal structure of R. miehei beta-mannanase (RmMan5A) was determined at a resolution of 2.3 A. Both RmMan5A and RmMan5B adopt the (beta/alpha)8-barrel architecture, which is globally similar to the other members of GH family 5. However, RmMan5B shows several differences in the loop around the active site. The extended loop between strand beta8 and helix alpha8 (residues 354-392) forms a `double' steric barrier to `block' the substrate-binding cleft at the end of the -1 subsite. Trp119, Asn260 and Glu380 in the beta-mannosidase, which are involved in hydrogen-bond contacts with the -1 mannose, might be essential for exo catalytic activity. Moreover, the structure of RmMan5B in complex with mannosyl-fructose has provided evidence for the interactions between the beta-mannosidase and D-fructofuranose. Overall, the present study not only helps in understanding the catalytic mechanism of GH family 5 beta-mannosidases, but also provides a basis for further enzymatic engineering of beta-mannosidases and beta-mannanases. Structural insights into the substrate specificity and transglycosylation activity of a fungal glycoside hydrolase family 5 beta-mannosidase.,Zhou P, Liu Y, Yan Q, Chen Z, Qin Z, Jiang Z Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2970-82. doi:, 10.1107/S1399004714019762. Epub 2014 Oct 23. PMID:25372687 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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