7fip

The native structure of beta-1,2-mannobiose phosphorylase from Thermoanaerobacter sp.

spinqualitylabelsall models 7fip, resolution 2.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7fip is a 4 chain structure with sequence from Thermoanaerobacter sp. X514. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.39Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BMBP_THEPX Probably involved in a salvage pathway for GDP-D-mannose biosynthesis (PubMed:25500577). Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan. In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate. Produces alpha-D-mannose 1-phosphate, which is the precursor of GDP-D-mannose (PubMed:25500577). Publication Abstract from PubMed 1,2-beta-Mannobiose phosphorylases (1,2-beta-MBPs) from glycoside hydrolase 130 (GH130) family are important bio-catalysts in glycochemistry applications owing to their ability in synthesizing oligomannans. Here, we report the crystal structure of a thermostable 1,2-beta-MBP from Thermoanaerobacter sp. X-514 termed Teth514_1789 to reveal the molecular basis of its higher thermostability and mechanism of action. We also solved the enzyme complexes of mannose, mannose-1-phosphate (M1P) and 1,4-beta-mannobiose to manifest the enzyme-substrate interaction networks of three main subsites. Notably, a Zn ion that should be derived from crystallization buffer was found in the active site and coordinates the phosphate moiety of M1P. Nonetheless, this Zn-coordination should reflect an inhibitory status as supplementing Zn severely impairs the enzyme activity. These results indicate that the effects of metal ions should be taken into consideration when applying Teth514_1789 and other related enzymes. Based on the structure, a reliable model of Teth514_1788 that shares 61.7% sequence identity to Teth514_1789 but displays a different substrate preference was built. Analyzing the structural features of these two closely related enzymes, we hypothesized that the length of a loop fragment that covers the entrance of the catalytic center might regulate the substrate selectivity. In conclusion, these information provide in-depth understanding of GH130 1,2-beta-MBPs and should serve as an important guidance for enzyme engineering for further applications. Structural investigation of a thermostable 1,2-beta-mannobiose phosphorylase from Thermoanaerobacter sp. X-514.,Dai L, Chang Z, Yang J, Liu W, Yang Y, Chen CC, Zhang L, Huang JW, Sun Y, Guo RT Biochem Biophys Res Commun. 2021 Nov 19;579:54-61. doi:, 10.1016/j.bbrc.2021.09.046. Epub 2021 Sep 21. PMID:34587555 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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