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==Chimeric Glycosyltransferase for the generation of novel natural products - GtfAH1 in complex with UDP-2F-Glc== | ==Chimeric Glycosyltransferase for the generation of novel natural products - GtfAH1 in complex with UDP-2F-Glc== | ||
<StructureSection load='3h4t' size='340' side='right' caption='[[3h4t]], [[Resolution|resolution]] 1.15Å' scene=''> | <StructureSection load='3h4t' size='340' side='right'caption='[[3h4t]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3h4t]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3h4t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinoplanes_teichomyceticus"_parenti_et_al._1978 "actinoplanes teichomyceticus" parenti et al. 1978]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H4T FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h4i|3h4i]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3h4i|3h4i]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GtfA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GtfA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1867 "Actinoplanes teichomyceticus" Parenti et al. 1978])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4t OCA], [https://pdbe.org/3h4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h4t RCSB], [https://www.ebi.ac.uk/pdbsum/3h4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h4t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 13: | Line 13: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h4/3h4t_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h4/3h4t_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Glycosyltransferase|Glycosyltransferase]] | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Actinoplanes teichomyceticus parenti et al. 1978]] | [[Category: Actinoplanes teichomyceticus parenti et al. 1978]] | ||
[[Category: Large Structures]] | |||
[[Category: Blundell, T L]] | [[Category: Blundell, T L]] | ||
[[Category: Dias, M V.B]] | [[Category: Dias, M V.B]] | ||
Revision as of 11:03, 16 March 2022
Chimeric Glycosyltransferase for the generation of novel natural products - GtfAH1 in complex with UDP-2F-GlcChimeric Glycosyltransferase for the generation of novel natural products - GtfAH1 in complex with UDP-2F-Glc
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlycodiversification, an invaluable tool for generating biochemical diversity, can be catalyzed by glycosyltransferases, which attach activated sugar "donors" onto "acceptor" molecules. However, many glycosyltransferases can tolerate only minor modifications to their native substrates, thus making them unsuitable tools for current glycodiversification strategies. Here we report the production of functional chimeric glycosyltransferases by mixing and matching the N- and C-terminal domains of glycopeptide glycosyltransferases. Using this method we have generated hybrid glycopeptides and have demonstrated that domain swapping can result in a predictable switch of substrate specificity, illustrating that N- and C-terminal domains predominantly dictate acceptor and donor specificity, respectively. The determination of the structure of a chimera in complex with a sugar donor analog shows that almost all sugar-glycosyltransferase binding interactions occur in the C-terminal domain. Chimeric glycosyltransferases for the generation of hybrid glycopeptides.,Truman AW, Dias MV, Wu S, Blundell TL, Huang F, Spencer JB Chem Biol. 2009 Jun 26;16(6):676-85. PMID:19549605[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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