3int | pdb_00003int

Structure of UDP-galactopyranose mutase bound to UDP-galactose (reduced)

spinqualitylabelsall models 3int, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3int is a 2 chain structure with sequence from "bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FDA, GDU, UDP Related: 1i8t, 2bi7, 2bi8, 1wam, 1v0j, 3gf4, 3inr Gene: glf, rfbD ("Bacillus pneumoniae" (Schroeter 1886) Flugge 1886) Activity: UDP-galactopyranose mutase, with EC number 5.4.99.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLF1_KLEPN] Involved in the biosynthesis of the galactose-containing O-side-chain polysaccharide backbone structure of D-galactan I which is a key component of lipopolysaccharide (LPS). Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is the biosynthetic precursor of galactofuranosyl residues. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The flavoenzyme uridine 5'-diphosphate galactopyranose mutase (UGM or Glf) catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose. The latter is a key building block for cell wall construction in numerous pathogens, including Mycobacterium tuberculosis. Mechanistic studies of UGM suggested a novel role for the flavin, and we previously provided evidence that the catalytic mechanism proceeds through a covalent flavin-galactose iminium. Here, we describe 2.3 and 2.5 A resolution X-ray crystal structures of the substrate-bound enzyme in oxidized and reduced forms, respectively. In the latter, C1 of the substrate is 3.6 A from the nucleophilic flavin N5 position. This orientation is consistent with covalent catalysis by flavin. X-ray Crystallography Reveals a Reduced Substrate Complex of UDP-Galactopyranose Mutase Poised for Covalent Catalysis by Flavin .,Gruber TD, Westler WM, Kiessling LL, Forest KT Biochemistry. 2009 Sep 10. PMID:19719175 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UDP-galactopyranose mutase UDP-galactopyranose mutase 3D structures

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