2j65
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STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP
OverviewOverview
The structure of recombinant Aquifex aeolicus, UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) in complex with UDP, has been determined to a resolution of 2.2 A. Previous studies have, characterized the binding sites of the fatty-acid and sugar moieties of, the substrate, UDP-(3-O-hydroxymyristoyl)-N-acetylglucosamine, but not, that of the nucleotide. The uracil-binding site is constructed from amino, acids that are highly conserved across species. Hydrophobic associations, with the Phe155 and Arg250 side chains in combination with, hydrogen-bonding interactions with the main chain of Glu154 and the side, chains of Tyr151 and Lys227 position the base. The phosphate and ribose, groups are directed away from the active site and interact with Arg137, Lys156, Glu186 and Arg250. The ... [(full description)]
About this StructureAbout this Structure
2J65 is a [Single protein] structure of sequence from [Aquifex aeolicus] with ZN, CL, MYR and UDP as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
The nucleotide-binding site of Aquifex aeolicus LpxC., Buetow L, Dawson A, Hunter WN, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1082-6. Epub 2006 Oct 25. PMID:17077484
Page seeded by OCA on Mon Oct 29 16:58:23 2007