2iw1

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[[Image:2iw1.gif|left|200px]]<br /><applet load="2iw1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2iw1.gif|left|200px]]
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caption="2iw1, resolution 1.50&Aring;" />
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'''CRYSTAL STRUCTURE OF WAAG, A GLYCOSYLTRANSFERASE INVOLVED IN LIPOPOLYSACCHARIDE BIOSYNTHESIS'''<br />
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{{Structure
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|PDB= 2iw1 |SIZE=350|CAPTION= <scene name='initialview01'>2iw1</scene>, resolution 1.50&Aring;
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|SITE= <scene name='pdbsite=AC1:U2f+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=U2F:URIDINE-5'-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE'>U2F</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF WAAG, A GLYCOSYLTRANSFERASE INVOLVED IN LIPOPOLYSACCHARIDE BIOSYNTHESIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IW1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=U2F:'>U2F</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:U2f+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IW1 OCA].
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2IW1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IW1 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17113996 17113996]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17113996 17113996]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: glycosyltransferase]]
[[Category: glycosyltransferase]]
[[Category: lipopolysaccharide biosynthesis]]
[[Category: lipopolysaccharide biosynthesis]]
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[[Category: lps]]
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[[Category: lp]]
[[Category: retaining]]
[[Category: retaining]]
[[Category: transferase]]
[[Category: transferase]]
[[Category: udp-glucose]]
[[Category: udp-glucose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:34:05 2008''

Revision as of 15:34, 20 March 2008


PDB ID 2iw1

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, resolution 1.50Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



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 therapeutic significance of the two enzymes.

About this Structure

2IW1 is a Single protein structure of sequence from Escherichia coli. 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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