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

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== Function ==
== Function ==
'''UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase'''
'''UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase'''
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(LpxD) is involved in 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>.
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(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 ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
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The <scene name='74/749395/Cv/6'>substrate-binding site</scene> of LpxA interacts with the substrate UDP moiety and the Glc-NAc moiety. It contains a <scene name='74/749395/Cv/7'>His-Asp catalytic dyad</scene> where the His acts as a general base and Asp helps to orient the His for participation in the catalysis<ref>PMID:17434525</ref>.
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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<ref>PMID:31664082</ref>.
</StructureSection>
</StructureSection>

Revision as of 08:09, 28 January 2021

UDP-3-O-(3-hydroxymyristoyl)glucosamine acyltransferase complex with Naphthalene derivative, DMSO and Mg+2 (PDB code 6uec)

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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

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