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Structure of LPXI D225A MutantStructure of LPXI D225A Mutant
Structural highlights
Publication Abstract from PubMedEnzymes in lipid metabolism acquire and deliver hydrophobic substrates and products from within lipid bilayers. The structure at 2.55 A of one isozyme of a constitutive enzyme in lipid A biosynthesis, LpxI from Caulobacter crescentus, has a novel fold. Two domains close around a completely sequestered substrate, UDP-2,3-diacylglucosamine, and open to release products either to the neighboring enzyme in a putative multienzyme complex or to the bilayer. Mutation analysis identifies Asp225 as key to Mg(2+)-catalyzed diphosphate hydrolysis. These structures provide snapshots of the enzymatic synthesis of a critical lipid A precursor. LpxI structures reveal how a lipid A precursor is synthesized.,Metzger LE 4th, Lee JK, Finer-Moore JS, Raetz CR, Stroud RM Nat Struct Mol Biol. 2012 Nov;19(11):1132-8. doi: 10.1038/nsmb.2393. Epub 2012, Oct 7. PMID:23042606[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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