5W8S

Lipid A Disaccharide Synthase (LpxB)-7 solubilizing mutations

Summary for 5W8S

• Entry DOI: 10.2210/pdb5w8s/pdb
• Related: 5W8N 5W8X
• Descriptor: Lipid-A-disaccharide synthase, SODIUM ION, LITHIUM ION, ... (4 entities in total)
• Functional Keywords: glycosyltransferase b, rossmann-like, c-terminal swap, dimer, lipid a disaccharide synthase, raetz pathway, lipid a synthesis pathway, lipiopolysaccharide synthesis, transferase
• Biological source: Escherichia coli BL21(DE3)
• Total number of polymer chains: 1
• Total formula weight: 42334.80

Authors

Bohl, T.E.,Aihara, H.,Shi, K.,Lee, J.K. (deposition date: 2017-06-22, release date: 2018-01-31, Last modification date: 2024-03-13)

Primary citation

Bohl, T.E.,Shi, K.,Lee, J.K.,Aihara, H.
Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli.
Nat Commun, 9:377-377, 2018

PubMed Abstract: 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.

PubMed: 29371662
DOI: 10.1038/s41467-017-02712-9

Experimental method

X-RAY DIFFRACTION (2.1 Å)