2iv3

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{{STRUCTURE_2iv3| PDB=2iv3 | SCENE= }}
{{STRUCTURE_2iv3| PDB=2iv3 | SCENE= }}
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'''CRYSTAL STRUCTURE OF AVIGT4, A GLYCOSYLTRANSFERASE INVOLVED IN AVILAMYCIN A BIOSYNTHESIS'''
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===CRYSTAL STRUCTURE OF AVIGT4, A GLYCOSYLTRANSFERASE INVOLVED IN AVILAMYCIN A BIOSYNTHESIS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17113996 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17113996}}
==About this Structure==
==About this Structure==
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[[Category: Glycosyltransferase]]
[[Category: Glycosyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 21:51, 27 July 2008

Image:2iv3.png

Template:STRUCTURE 2iv3

CRYSTAL STRUCTURE OF AVIGT4, A GLYCOSYLTRANSFERASE INVOLVED IN AVILAMYCIN A BIOSYNTHESIS

Template:ABSTRACT PUBMED 17113996

About this Structure

2IV3 is a Single protein structure of sequence from Streptomyces viridochromogenes. 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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