2iuy

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[[Image:2iuy.gif|left|200px]]
 
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{{Structure
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==Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis==
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|PDB= 2iuy |SIZE=350|CAPTION= <scene name='initialview01'>2iuy</scene>, resolution 2.10&Aring;
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<StructureSection load='2iuy' size='340' side='right'caption='[[2iuy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Mes+Binding+Site+For+Chain+A'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[2iuy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUY FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iuy OCA], [https://pdbe.org/2iuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iuy RCSB], [https://www.ebi.ac.uk/pdbsum/2iuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iuy ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iuy OCA], [http://www.ebi.ac.uk/pdbsum/2iuy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iuy RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q93KV2_STRVR Q93KV2_STRVR]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iu/2iuy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2iuy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''CRYSTAL STRUCTURE OF AVIGT4, A GLYCOSYLTRANSFERASE INVOLVED IN AVILAMYCIN A BIOSYNTHESIS'''
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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:17113996<ref>PMID:17113996</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2iuy" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2IUY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUY OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Single protein]]
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[[Category: Streptomyces viridochromogenes]]
[[Category: Streptomyces viridochromogenes]]
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[[Category: Bolam, D N.]]
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[[Category: Bolam DN]]
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[[Category: Davies, G J.]]
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[[Category: Davies GJ]]
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[[Category: Gilbert, H J.]]
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[[Category: Gilbert HJ]]
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[[Category: Martinez-Fleites, C.]]
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[[Category: Martinez-Fleites C]]
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[[Category: Proctor, M.]]
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[[Category: Proctor M]]
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[[Category: Roberts, S.]]
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[[Category: Roberts S]]
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[[Category: antibiotic]]
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[[Category: avilamycin some]]
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[[Category: family gt-4]]
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[[Category: glycosyltransferase]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:00 2008''
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Current revision

Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis

PDB ID 2iuy

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