8id7 | pdb_00008id7

Crystal structure of YbiW in complex with 1,5-anhydroglucitol-6-phosphate in Escherichia coli

spinqualitylabelsall models 8id7, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8id7 is a 1 chain structure with sequence from Escherichia coli str. K-12 substr. MG1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.65Å Ligands: 0WK Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GRE2_ECOLI Probably shows dehydratase activity. Publication Abstract from PubMed Glycyl radical enzymes (GREs) catalyze mechanistically diverse radical-mediated reactions, playing important roles in the metabolism of anaerobic bacteria. The model bacterium Escherichia coli MG1655 contains two GREs of unknown function, YbiW and PflD, which are widespread among human intestinal bacteria. Here, we report that YbiW and PflD catalyze ring-opening C-O cleavage of 1,5-anhydroglucitol-6-phosphate (AG6P) and 1,5-anhydromannitol-6-phosphate (AM6P), respectively. The product of both enzymes, 1-deoxy-fructose-6-phosphate (DF6P), is then cleaved by the aldolases FsaA or FsaB to form glyceraldehyde-3-phosphate (G3P) and hydroxyacetone (HA), which are then reduced by the NADH-dependent dehydrogenase GldA to form 1,2-propanediol (1,2-PDO). Crystal structures of YbiW and PflD in complex with their substrates provided insights into the mechanism of radical-mediated C-O cleavage. This "anhydroglycolysis" pathway enables anaerobic growth of E. coli on 1,5-anhydroglucitol (AG) and 1,5-anhydromannitol (AM), and we probe the feasibility of harnessing this pathway for the production of 1,2-PDO, a highly demanded chiral chemical feedstock, from inexpensive starch. Discovery of the anhydroglycolysis pathway expands the known catalytic repertoire of GREs, clarifies the hitherto unknown physiological functions of the well-studied enzymes FsaA, FsaB, and GldA, and demonstrates how enzyme discovery efforts can cast light on prevalent yet overlooked metabolites in the microbiome. A Widespread Radical-Mediated Glycolysis Pathway.,Ma K, Xue B, Chu R, Zheng Y, Sharma S, Jiang L, Hu M, Xie Y, Hu Y, Tao T, Zhou Y, Liu D, Li Z, Yang Q, Chen Y, Wu S, Tong Y, Robinson RC, Yew WS, Jin X, Liu Y, Zhao H, Ang EL, Wei Y, Zhang Y J Am Chem Soc. 2024 Sep 25;146(38):26187-26197. doi: 10.1021/jacs.4c07718. Epub , 2024 Sep 16. PMID:39283600 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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