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Nat Struct Mol Biol. 2012 Nov;19(11):1132-8. doi: 10.1038/nsmb.2393. Epub 2012 Oct 7.

LpxI structures reveal how a lipid A precursor is synthesized.

Author information

1
Department of Biochemistry and Biophysics, The University of California San Francisco, San Francisco, California, USA. metzger@msg.ucsf.edu

Abstract

Enzymes in lipid metabolism acquire and deliver hydrophobic substrates and products from within lipid bilayers. The structure at 2.55 Å 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.

PMID:
23042606
PMCID:
PMC3562136
DOI:
10.1038/nsmb.2393
[Indexed for MEDLINE]
Free PMC Article
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