2IV7

Crystal Structure of WaaG, a glycosyltransferase involved in lipopolysaccharide biosynthesis

Summary for 2IV7

• Entry DOI: 10.2210/pdb2iv7/pdb
• Related: 2IW1
• Descriptor: LIPOPOLYSACCHARIDE CORE BIOSYNTHESIS PROTEIN RFAG, URIDINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: lipopolysaccharide biosynthesis, lps, transferase, family gt-4, glycosyltransferase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 43072.47

Authors

Martinez-Fleites, C.,Proctor, M.,Roberts, S.,Bolam, D.N.,Gilbert, H.J.,Davies, G.J. (deposition date: 2006-06-08, release date: 2006-10-11, Last modification date: 2024-10-16)

Primary citation

Martinez-Fleites, C.,Proctor, M.,Roberts, S.,Bolam, D.N.,Gilbert, H.J.,Davies, G.J.
Insights Into the Synthesis of Lipopolysaccharide and Antibiotics Through the Structures of Two Retaining Glycosyltransferases from Family Gt4
Chem.Biol., 13:1143-, 2006

PubMed Abstract: Glycosyltransferases (GTs) catalyze the synthesis of the myriad glycoconjugates that are central to life. One of the largest families is GT4, which contains several enzymes of therapeutic significance, exemplified by WaaG and AviGT4. WaaG catalyses a key step in lipopolysaccharide synthesis, while AviGT4, produced by Streptomyces viridochromogenes, contributes to the synthesis of the antibiotic avilamycin A. Here we present the crystal structure of both WaaG and AviGT4. The two enzymes contain two "Rossmann-like" (beta/alpha/beta) domains characteristic of the GT-B fold. Both recognition of the donor substrate and the catalytic machinery is similar to other retaining GTs that display the GT-B fold. Structural information is discussed with respect to the evolution of GTs and the therapeutic significance of the two enzymes.

PubMed: 17113996
DOI: 10.1016/J.CHEMBIOL.2006.09.005

Experimental method

X-RAY DIFFRACTION (1.6 Å)