2iv7
From Proteopedia
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|PDB= 2iv7 |SIZE=350|CAPTION= <scene name='initialview01'>2iv7</scene>, resolution 1.60Å | |PDB= 2iv7 |SIZE=350|CAPTION= <scene name='initialview01'>2iv7</scene>, resolution 1.60Å | ||
|SITE= <scene name='pdbsite=AC1:Udp+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Udp+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iv7 OCA], [http://www.ebi.ac.uk/pdbsum/2iv7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iv7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Proctor, M.]] | [[Category: Proctor, M.]] | ||
[[Category: Roberts, S.]] | [[Category: Roberts, S.]] | ||
| - | [[Category: UDP]] | ||
[[Category: family gt-4]] | [[Category: family gt-4]] | ||
[[Category: glycosyltransferase]] | [[Category: glycosyltransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:09 2008'' |
Revision as of 00:49, 31 March 2008
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| , resolution 1.60Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
2IV7 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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