UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models UDP-3-O-(3-hydroxymyristoyl)glucosamine acyltransferase complex with Naphthalene derivative, DMSO and Mg+2 (PDB code 6uec) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase or UDP-3-O-acylglucosamine N-acyltransferase (LpxD) is involved in the third step of the biosynthesis of lipid A which is a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Thus, LpxD is essential to survival of Gram-negative bacteria. It catalyzes the N-acylation of UDP-3-O-(3-hydroxytetradeanoyl)glucosamine[1]. LpxD is structurally similar to LpxA which functions as the first enzye in the lipid A biosynthesis. Relevance LpxD inhibitors are antimicrobials[2]. Structural highlights The biological assembly of UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase is (PDB code 6uec). The 3D structure of LpxD complex with a ligand shows the binding site to be situated at the interface of the crystallographic dimer. There are extensive polar interactions with LpxD as well as hydrogen bonds with the adjacent monomer[3].

3D structures of UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

Updated on 28-January-2021

References

1. ↑ Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J Bacteriol. 2008 Jul;190(13):4549-58. doi: 10.1128/JB.00234-08. Epub 2008 May 2. PMID:18456814 doi:http://dx.doi.org/10.1128/JB.00234-08
2. ↑ Jenkins RJ, Dotson GD. Dual targeting antibacterial peptide inhibitor of early lipid A biosynthesis. ACS Chem Biol. 2012 Jul 20;7(7):1170-7. doi: 10.1021/cb300094a. Epub 2012 Apr 27. PMID:22530734 doi:http://dx.doi.org/10.1021/cb300094a
3. ↑ Kroeck KG, Sacco MD, Smith EW, Zhang X, Shoun D, Akhtar A, Darch SE, Cohen F, Andrews LD, Knox JE, Chen Y. Discovery of dual-activity small-molecule ligands of Pseudomonas aeruginosa LpxA and LpxD using SPR and X-ray crystallography. Sci Rep. 2019 Oct 29;9(1):15450. doi: 10.1038/s41598-019-51844-z. PMID:31664082 doi:http://dx.doi.org/10.1038/s41598-019-51844-z