2iw1
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(New page: 200px<br /> <applet load="2iw1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iw1, resolution 1.50Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:06, 29 October 2007
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CRYSTAL STRUCTURE OF WAAG, A GLYCOSYLTRANSFERASE INVOLVED IN LIPOPOLYSACCHARIDE 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 ... [(full description)]
About this Structure
2IW1 is a [Single protein] structure of sequence from [Escherichia coli] with U2F as [ligand]. 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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