Structural highlights
Function
A0A0H3C8Q1_CAUVN
Publication Abstract from PubMed
Enzymes 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
- ↑ Metzger LE 4th, Lee JK, Finer-Moore JS, Raetz CR, Stroud RM. LpxI structures reveal how a lipid A precursor is synthesized. Nat Struct Mol Biol. 2012 Nov;19(11):1132-8. doi: 10.1038/nsmb.2393. Epub 2012, Oct 7. PMID:23042606 doi:http://dx.doi.org/10.1038/nsmb.2393