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PDBsum entry 4j6e
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References listed in PDB file
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Key reference
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Title
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Lpxi structures reveal how a lipid a precursor is synthesized.
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Authors
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L.E.Metzger,
J.K.Lee,
J.S.Finer-Moore,
C.R.Raetz,
R.M.Stroud.
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Ref.
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Nat Struct Biol, 2012,
19,
1132-1138.
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PubMed id
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Abstract
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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.
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