3ps2 | pdb_00003ps2

Crystal structure of the Escherichia Coli LPXC/LPC-012 complex

spinqualitylabelsall models 3ps2, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ps2 is a 1 chain structure with sequence from Ecoki. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DMS, SO4, UKW, ZH4, ZN Related: 3ps1, 3ps3 Gene: ECOK1_0097, ENVA, lpxC (ECOKI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [D5CV28_ECOKI] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (By similarity).[HAMAP-Rule:MF_00388][SAAS:SAAS004463_004_013136] Publication Abstract from PubMed Compounds inhibiting LpxC in the lipid A biosynthetic pathway are promising leads for novel antibiotics against multidrug-resistant Gram-negative pathogens. We report the syntheses and structural and biochemical characterizations of LpxC inhibitors based on a diphenyl-diacetylene (1,4-diphenyl-1,3-butadiyne) threonyl-hydroxamate scaffold. These studies provide a molecular interpretation for the differential antibiotic activities of compounds with a substituted distal phenyl ring as well as the absolute stereochemical requirement at the C2, but not C3, position of the threonyl group. Syntheses, structures and antibiotic activities of LpxC inhibitors based on the diacetylene scaffold.,Liang X, Lee CJ, Chen X, Chung HS, Zeng D, Raetz CR, Li Y, Zhou P, Toone EJ Bioorg Med Chem. 2011 Jan 15;19(2):852-60. Epub 2010 Dec 9. PMID:21194954 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UDP-3-O-acyl-N-acetylglucosamine deacetylase

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