5w8x

Lipid A Disaccharide Synthase (LpxB)-7 solubilizing mutations-Bound to UDP

spinqualitylabelsall models 5w8x, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5w8x is a 1 chain structure with sequence from Ecobd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UDP Related: 5w8s, 5w8n Gene: lpxB, ECBD_3437 (ECOBD) Activity: Lipid-A-disaccharide synthase, with EC number 2.4.1.182 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A140NAT1_ECOBD] Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[HAMAP-Rule:MF_00392][SAAS:SAAS00702254] Publication Abstract from PubMed Most Gram-negative bacteria are surrounded by a glycolipid called lipopolysaccharide (LPS), which forms a barrier to hydrophobic toxins and, in pathogenic bacteria, is a virulence factor. During LPS biosynthesis, a membrane-associated glycosyltransferase (LpxB) forms a tetra-acylated disaccharide that is further acylated to form the membrane anchor moiety of LPS. Here we solve the structure of a soluble and catalytically competent LpxB by X-ray crystallography. The structure reveals that LpxB has a glycosyltransferase-B family fold but with a highly intertwined, C-terminally swapped dimer comprising four domains. We identify key catalytic residues with a product, UDP, bound in the active site, as well as clusters of hydrophobic residues that likely mediate productive membrane association or capture of lipidic substrates. These studies provide the basis for rational design of antibiotics targeting a crucial step in LPS biosynthesis. Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli.,Bohl TE, Shi K, Lee JK, Aihara H Nat Commun. 2018 Jan 25;9(1):377. doi: 10.1038/s41467-017-02712-9. PMID:29371662 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA