UDP-N-acetylglucosamine acyltransferase

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Revision as of 12:49, 8 June 2017

spinqualitylabelsall models E. coli UDP-N-acetylglucosamine acyltransferase complex with UDP-Glc-NAC (PDB code 2jf3) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function UDP-N-acetylglucosamine acyltransferase (LpxA) initiates lipid A biosynthesis. It catalyzes the transfer of 3-hydroxymyristic acid from acyl carrier protein to the 3'-hydroxyl group of UDP-GlcNAc[1]. Structural highlights The substrate-binding site of LpxA ainteracts with the substrate UDP moiety and the Glc-NAc moiety. It contains a His-Asp catalytic dyad where the His acts as a general base and Asp helps to orient the His for participation in the catalysis[2].

3D structures of UDP-N-acetylglucosamine acyltransferase

Updated on 08-June-2017

References

1. ↑ Wyckoff TJ, Raetz CR. The active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis. J Biol Chem. 1999 Sep 17;274(38):27047-55. PMID:10480918
2. ↑ Ulaganathan V, Buetow L, Hunter WN. Nucleotide substrate recognition by UDP-N-acetylglucosamine acyltransferase (LpxA) in the first step of lipid A biosynthesis. J Mol Biol. 2007 Jun 1;369(2):305-12. Epub 2007 Mar 21. PMID:17434525 doi:10.1016/j.jmb.2007.03.039