4ggm

Structure of LpxIStructure of LpxI

Structural highlights 4ggm is a 1 chain structure with sequence from Caulobacter vibrioides NA1000. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.897Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 4ggm, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image