2iv3
From Proteopedia
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CRYSTAL STRUCTURE OF AVIGT4, A GLYCOSYLTRANSFERASE INVOLVED IN AVILAMYCIN A BIOSYNTHESIS
Overview
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.
About this Structure
2IV3 is a Single protein structure of sequence from Streptomyces viridochromogenes with UDP and GOL as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4., Martinez-Fleites C, Proctor M, Roberts S, Bolam DN, Gilbert HJ, Davies GJ, Chem Biol. 2006 Nov;13(11):1143-52. PMID:17113996
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