5jxx

Crystal structure of UDP-N-acetylglucosamine O-acyltransferase (LpxA) from Moraxella catarrhalis RH4.

spinqualitylabelsall models 5jxx, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jxx is a 6 chain structure with sequence from Moraxella catarrhalis BBH18. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.001Å Ligands: FLC, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D5VAW8_MORCB Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[HAMAP-Rule:MF_00387][SAAS:SAAS00720115] Publication Abstract from PubMed Lipopolysaccharide (LPS) is an important surface component and a potential virulence factor in the pathogenesis of Gram-negative bacteria. UDP-N-acetylglucosamine acyltransferase (LpxA) enzyme catalyzes the first reaction of LPS biosynthesis, reversible transfer of R-3-hydroxy-acyl moiety from donor R-3-hydroxy-acyl-acyl carrier protein to the 3' hydroxyl position of UDP-N-acetyl-glucosamine. LpxA enzyme's essentiality in bacterial survival and absence of any homologous protein in humans makes it a promising target for anti-bacterial drug development. Herein, we present the crystal structure of Moraxella catarrhalis LpxA (McLpxA). We propose that L171 is responsible for limiting the acyl chain length in McLpxA to 10C or 12C. The study reveals the plausible interactions between the highly conserved clusters of basic residues at the C-terminal end of McLpxA and acidic residues of acyl carrier protein (ACP). Furthermore, the crystal structure of McLpxA was used to screen potential inhibitors from NCI open database using various computational approaches viz. pharmacophore mapping, virtual screening and molecular docking. Molecules Mol212032, Mol609399 and Mol152546 showed best binding affinity with McLpxA among all screened molecules. These molecules mimic the substrate-LpxA binding interactions. Acyl chain preference and inhibitor identification of Moraxella catarrhalis LpxA: Insight through crystal structure and computational studies.,Pratap S, Kesari P, Yadav R, Dev A, Narwal M, Kumar P Int J Biol Macromol. 2017 Mar;96:759-765. doi: 10.1016/j.ijbiomac.2017.01.005., Epub 2017 Jan 3. PMID:28057571 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UDP-N-acetylglucosamine acyltransferase

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