5zye

Crystal Structure of Glucose Isomerase Soaked with Mn2+ and Glucose

spinqualitylabelsall models 5zye, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zye is a 1 chain structure with sequence from Streptomyces rubiginosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: GLC, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function XYLA_STRRU Involved in D-xylose catabolism. Publication Abstract from PubMed Glucose isomerase (GI) catalyzes the reversible enzymatic isomerization of d-glucose and d-xylose to d-fructose and d-xylulose, respectively. This is one of the most important enzymes in the production of high-fructose corn syrup (HFCS) and biofuel. We recently determined the crystal structure of GI from S. rubiginosus (SruGI) complexed with a xylitol inhibitor in one metal binding mode. Although we assessed inhibitor binding at the M1 site, the metal binding at the M2 site and the substrate recognition mechanism for SruGI remains the unclear. Here, we report the crystal structure of the two metal binding modes of SruGI and its complex with glucose. This study provides a snapshot of metal binding at the SruGI M2 site in the presence of Mn(2+), but not in the presence of Mg(2+). Metal binding at the M2 site elicits a configuration change at the M1 site. Glucose molecule can only bind to the M1 site in presence of Mn(2+) at the M2 site. Glucose and Mn(2+) at the M2 site were bridged by water molecules using a hydrogen bonding network. The metal binding geometry of the M2 site indicates a distorted octahedral coordination with an angle of 55-110 degrees , whereas the M1 site has a relatively stable octahedral coordination with an angle of 85-95 degrees . We suggest a two-step sequential process for SruGI substrate recognition, in Mn(2+) binding mode, at the M2 site. Our results provide a better understanding of the molecular role of the M2 site in GI substrate recognition. Structural analysis of substrate recognition by glucose isomerase in Mn(2+) binding mode at M2 site in S. rubiginosus.,Bae JE, Hwang KY, Nam KH Biochem Biophys Res Commun. 2018 Sep 5;503(2):770-775. doi:, 10.1016/j.bbrc.2018.06.074. Epub 2018 Jun 18. PMID:29909012 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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