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2iv7
From Proteopedia
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| - | [[Image:2iv7.png|left|200px]] | ||
| - | + | ==Crystal Structure of WaaG, a glycosyltransferase involved in lipopolysaccharide biosynthesis== | |
| + | <StructureSection load='2iv7' size='340' side='right'caption='[[2iv7]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2iv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecow3 Ecow3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IV7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iw1|2iw1]]</div></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iv7 OCA], [https://pdbe.org/2iv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iv7 RCSB], [https://www.ebi.ac.uk/pdbsum/2iv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iv7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/RFAG_ECOLI RFAG_ECOLI]] Involved in the addition of the first glucose residue to the lipopolysaccharide core. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/2iv7_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2iv7 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:17113996</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2iv7" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Glycosyltransferase|Glycosyltransferase]] | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Bolam, D N | + | [[Category: Ecow3]] |
| - | [[Category: Davies, G J | + | [[Category: Large Structures]] |
| - | [[Category: Gilbert, H J | + | [[Category: Bolam, D N]] |
| - | [[Category: Martinez-Fleites, C | + | [[Category: Davies, G J]] |
| - | [[Category: Proctor, M | + | [[Category: Gilbert, H J]] |
| - | [[Category: Roberts, S | + | [[Category: Martinez-Fleites, C]] |
| + | [[Category: Proctor, M]] | ||
| + | [[Category: Roberts, S]] | ||
[[Category: Family gt-4]] | [[Category: Family gt-4]] | ||
[[Category: Glycosyltransferase]] | [[Category: Glycosyltransferase]] | ||
Current revision
Crystal Structure of WaaG, a glycosyltransferase involved in lipopolysaccharide biosynthesis
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