6zj4: Difference between revisions
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==apo-Trehalose transferase (apo-TreT) from Thermoproteus uzoniensis== | ==apo-Trehalose transferase (apo-TreT) from Thermoproteus uzoniensis== | ||
<StructureSection load='6zj4' size='340' side='right'caption='[[6zj4]]' scene=''> | <StructureSection load='6zj4' size='340' side='right'caption='[[6zj4]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZJ4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6zj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoproteus_uzoniensis Thermoproteus uzoniensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZJ4 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=6zj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zj4 OCA], [https://pdbe.org/6zj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zj4 RCSB], [https://www.ebi.ac.uk/pdbsum/6zj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zj4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/F2L613_THEU7 F2L613_THEU7] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Retaining LeLoir glycosyltransferases catalyze the formation of glycosidic bonds between nucleotide sugar donors and carbohydrate acceptors. The anomeric selectivity of trehalose transferase from Thermoproteus uzoniensis was investigated for both d- and l-glycopyranose acceptors. The enzyme couples a wide range of carbohydrates, yielding trehalose analogues with conversion and enantioselectivity of >98%. The anomeric selectivity inverts from alpha,alpha-(1 --> 1)-glycosidic bonds for d-glycopyranose acceptors to alpha,beta-(1 --> 1)-glycosidic bonds for l-glycopyranose acceptors, while (S)-selectivity was retained for both types of sugar acceptors. Comparison of protein crystal structures of trehalose transferase in complex with alpha,alpha-trehalose and an unnatural alpha,beta-trehalose analogue highlighted the mechanistic rationale for the observed inversion of anomeric selectivity. | |||
Anomeric Selectivity of Trehalose Transferase with Rare l-Sugars.,Mestrom L, Marsden SR, van der Eijk H, Laustsen JU, Jeffries CM, Svergun DI, Hagedoorn PL, Bento I, Hanefeld U ACS Catal. 2020 Aug 7;10(15):8835-8839. doi: 10.1021/acscatal.0c02117. Epub 2020 , Jul 22. PMID:32953231<ref>PMID:32953231</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6zj4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Thermoproteus uzoniensis]] | |||
[[Category: Bento I]] | [[Category: Bento I]] | ||
[[Category: Hagedoorn P-H]] | [[Category: Hagedoorn P-H]] | ||
