5JXX
Crystal structure of UDP-N-acetylglucosamine O-acyltransferase (LpxA) from Moraxella catarrhalis RH4.
Summary for 5JXX
| Entry DOI | 10.2210/pdb5jxx/pdb |
| Descriptor | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, GLYCEROL, CITRATE ANION, ... (4 entities in total) |
| Functional Keywords | udp-n-acetylglucosamine o-acyltransferase, lpxa, acyltransferase, transferase |
| Biological source | Moraxella catarrhalis (strain BBH18) |
| Cellular location | Cytoplasm : D5VAW8 |
| Total number of polymer chains | 6 |
| Total formula weight | 169631.49 |
| Authors | Pratap, S.,Kesari, P.,Yadav, R.,Narwal, M.,Dev, A.,Kumar, P. (deposition date: 2016-05-13, release date: 2017-06-14, Last modification date: 2023-11-08) |
| Primary citation | Pratap, S.,Kesari, P.,Yadav, R.,Dev, A.,Narwal, M.,Kumar, P. Acyl chain preference and inhibitor identification of Moraxella catarrhalis LpxA: Insight through crystal structure and computational studies. Int. J. Biol. Macromol., 96:759-765, 2017 Cited by PubMed Abstract: 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. PubMed: 28057571DOI: 10.1016/j.ijbiomac.2017.01.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.001 Å) |
Structure validation
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