3otg: Difference between revisions
New page: '''Unreleased structure''' The entry 3otg is ON HOLD Authors: Chang, A., Singh, S., Bingman, C.A., Thorson, J.S., Phillips Jr., G.N., Center for Eukaryotic Structural Genomics (CESG) D... |
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==Crystal Structure of CalG1, Calicheamicin Glycostyltransferase, TDP bound form== | |||
<StructureSection load='3otg' size='340' side='right'caption='[[3otg]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3otg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_echinospora Micromonospora echinospora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OTG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></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=3otg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3otg OCA], [https://pdbe.org/3otg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3otg RCSB], [https://www.ebi.ac.uk/pdbsum/3otg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3otg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8KNF2_MICEC Q8KNF2_MICEC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glycosyltransferases are useful synthetic catalysts for generating natural products with sugar moieties. Although several natural product glycosyltransferase structures have been reported, design principles of glycosyltransferase engineering for the generation of glycodiversified natural products has fallen short of its promise, partly due to a lack of understanding of the relationship between structure and function. Here, we report structures of all four calicheamicin glycosyltransferases (CalG1, CalG2, CalG3, and CalG4), whose catalytic functions are clearly regiospecific. Comparison of these four structures reveals a conserved sugar donor binding motif and the principles of acceptor binding region reshaping. Among them, CalG2 possesses a unique catalytic motif for glycosylation of hydroxylamine. Multiple glycosyltransferase structures in a single natural product biosynthetic pathway are a valuable resource for understanding regiospecific reactions and substrate selectivities and will help future glycosyltransferase engineering. | |||
Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity.,Chang A, Singh S, Helmich KE, Goff RD, Bingman CA, Thorson JS, Phillips GN Jr Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):17649-54. Epub 2011 Oct 10. PMID:21987796<ref>PMID:21987796</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3otg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Micromonospora echinospora]] | |||
[[Category: Bingman CA]] | |||
[[Category: Chang A]] | |||
[[Category: Phillips Jr GN]] | |||
[[Category: Singh S]] | |||
[[Category: Thorson JS]] | |||
Latest revision as of 12:31, 30 October 2024
Crystal Structure of CalG1, Calicheamicin Glycostyltransferase, TDP bound formCrystal Structure of CalG1, Calicheamicin Glycostyltransferase, TDP bound form
Structural highlights
FunctionPublication Abstract from PubMedGlycosyltransferases are useful synthetic catalysts for generating natural products with sugar moieties. Although several natural product glycosyltransferase structures have been reported, design principles of glycosyltransferase engineering for the generation of glycodiversified natural products has fallen short of its promise, partly due to a lack of understanding of the relationship between structure and function. Here, we report structures of all four calicheamicin glycosyltransferases (CalG1, CalG2, CalG3, and CalG4), whose catalytic functions are clearly regiospecific. Comparison of these four structures reveals a conserved sugar donor binding motif and the principles of acceptor binding region reshaping. Among them, CalG2 possesses a unique catalytic motif for glycosylation of hydroxylamine. Multiple glycosyltransferase structures in a single natural product biosynthetic pathway are a valuable resource for understanding regiospecific reactions and substrate selectivities and will help future glycosyltransferase engineering. Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity.,Chang A, Singh S, Helmich KE, Goff RD, Bingman CA, Thorson JS, Phillips GN Jr Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):17649-54. Epub 2011 Oct 10. PMID:21987796[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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