UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
From Proteopedia
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(New page: <StructureSection load='' size='350' side='right' caption='E. coli UDP-N-acetylglucosamine acyltransferase complex with UDP-Glc-NAC (PDB code 2jf3)' scene='74/749395/Cv/1'> == Functio...) |
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| - | <StructureSection load='' size='350' side='right' caption=' | + | <StructureSection load='6uec' size='350' side='right' caption='UDP-3-O-(3-hydroxymyristoyl)glucosamine acyltransferase complex with Naphthalene derivative, DMSO and Mg+2 (PDB code [[6uec]])' scene='87/873780/Cv/3'> |
== Function == | == Function == | ||
| - | '''UDP-3-O-(3-hydroxymyristoyl)glucosamine N- | + | '''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<ref>PMID:18456814</ref>. LpxD is structurally similar to LpxA which functions as the first enzye in the lipid A biosynthesis. | |
| - | ''' | + | |
| + | == Relevance == | ||
| + | LpxD inhibitors are antimicrobials<ref>PMID:22530734</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
| - | The <scene name=' | + | The biological assembly of UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase is <scene name='87/873780/Cv/4'>homotrimer</scene> (PDB code [[6uec]]). The 3D structure of LpxD complex with a ligand shows the binding site to be situated at <scene name='87/873780/Cv/6'>the interface of the crystallographic dimer</scene>. There are extensive polar interactions with LpxD as well as hydrogen bonds<ref>PMID:31664082</ref>. <scene name='87/873780/Cv/8'>Mg coordination site</scene>. Water molecules are shown as red spheres. |
</StructureSection> | </StructureSection> | ||
Current revision
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3D structures of UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
Updated on 31-January-2021
References
- ↑ 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
- ↑ 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
- ↑ 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
