UDP-N-acetylglucosamine acyltransferase
From Proteopedia
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| - | <StructureSection load='2jf3' size='340' side='right' caption='E. coli UDP-N-acetylglucosamine acyltransferase complex with UDP-Glc-NAC (PDB code [[2jf3]]' scene=''> | + | <StructureSection load='2jf3' size='340' side='right' caption='E. coli UDP-N-acetylglucosamine acyltransferase complex with UDP-Glc-NAC (PDB code [[2jf3]])' scene=''> |
== Function == | == 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<ref>PMID: | + | '''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<ref>PMID:10480918</ref>. |
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== Structural highlights == | == 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<ref>PMID:17434525</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 10:19, 25 December 2016
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3D structures of UDP-N-acetylglucosamine acyltransferase
Updated on 25-December-2016
References
- ↑ 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
- ↑ 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
