UDP-N-acetylglucosamine acyltransferase

(Difference between revisions)

Revision as of 12:04, 10 October 2019

E. coli UDP-N-acetylglucosamine acyltransferase complex with UDP-Glc-NAC (PDB code 2jf3)

Drag the structure with the mouse to rotate

Updated on 10-October-2019

↑ 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

@@ Line 5: / Line 5: @@
 == Structural highlights ==
-The <scene name='74/749395/Cv/4'>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/5'>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>.
+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>.
 </StructureSection>