5b0p | pdb_00005b0p

Beta-1,2-Mannobiose phosphorylase from Listeria innocua - glycerol complex

spinqualitylabelsall models 5b0p, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5b0p is a 2 chain structure with sequence from Listeria innocua Clip11262. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: GOL, MES, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BMBP_LISIN Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan (PubMed:26632508). In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate, but can also use beta-1,2-mannotriose (PubMed:26632508). Publication Abstract from PubMed Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for beta-mannosides. Here, we characterized beta-1,2-mannobiose phosphorylase from Listeria innocua (Lin0857) and determined its crystal structures complexed with beta-1,2-linked mannooligosaccharides. beta-1,2-Mannotriose was bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, and a significant open-close loop displacement was observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size. A structural basis for substrate recognition and phosphorolysis was provided. Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua.,Tsuda T, Nihira T, Chiku K, Suzuki E, Arakawa T, Nishimoto M, Kitaoka M, Nakai H, Fushinobu S FEBS Lett. 2015 Dec 21;589(24 Pt B):3816-21. doi: 10.1016/j.febslet.2015.11.034. , Epub 2015 Nov 26. PMID:26632508 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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