3iaa: Difference between revisions

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==Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP bound form==
==Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP bound form==
<StructureSection load='3iaa' size='340' side='right' caption='[[3iaa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3iaa' size='340' side='right'caption='[[3iaa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3iaa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15837 Atcc 15837]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IAA FirstGlance]. <br>
<table><tr><td colspan='2'>[[3iaa]] is a 2 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=3IAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IAA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.505&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ia7|3ia7]]</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=3iaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iaa OCA], [https://pdbe.org/3iaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iaa RCSB], [https://www.ebi.ac.uk/pdbsum/3iaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iaa ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calG2, Q8KNE0 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1877 ATCC 15837])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3iaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iaa OCA], [http://pdbe.org/3iaa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3iaa RCSB], [http://www.ebi.ac.uk/pdbsum/3iaa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3iaa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8KNE0_MICEC Q8KNE0_MICEC]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ia/3iaa_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ia/3iaa_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Glycosyltransferase|Glycosyltransferase]]
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 15837]]
[[Category: Large Structures]]
[[Category: Bingman, C A]]
[[Category: Micromonospora echinospora]]
[[Category: Chang, A]]
[[Category: Bingman CA]]
[[Category: Phillips, G N]]
[[Category: Chang A]]
[[Category: Singh, S]]
[[Category: Phillips Jr GN]]
[[Category: Thorson, J S]]
[[Category: Singh S]]
[[Category: Calg2]]
[[Category: Thorson JS]]
[[Category: Calicheamicin]]
[[Category: Enediyne]]
[[Category: Glycosyltransferase]]
[[Category: Tdp]]
[[Category: Transferase]]

Latest revision as of 13:00, 6 November 2024

Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP bound formCrystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP bound form

Structural highlights

3iaa is a 2 chain structure with sequence from Micromonospora echinospora. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.505Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8KNE0_MICEC

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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Chang A, Singh S, Helmich KE, Goff RD, Bingman CA, Thorson JS, Phillips GN Jr. Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity. Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):17649-54. Epub 2011 Oct 10. PMID:21987796 doi:10.1073/pnas.1108484108

3iaa, resolution 2.50Å

Drag the structure with the mouse to rotate

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