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6zj4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==apo-Trehalose transferase (apo-TreT) from Thermoproteus uzoniensis== | |
| + | <StructureSection load='6zj4' size='340' side='right'caption='[[6zj4]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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> | ||
| + | == 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> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bento | + | <div class="pdbe-citations 6zj4" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Hanefeld | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Thermoproteus uzoniensis]] |
| - | [[Category: | + | [[Category: Bento I]] |
| - | [[Category: Van | + | [[Category: Hagedoorn P-H]] |
| + | [[Category: Hanefeld U]] | ||
| + | [[Category: Jeffries CM]] | ||
| + | [[Category: Laustsen JU]] | ||
| + | [[Category: Marsden SR]] | ||
| + | [[Category: Mestrom L]] | ||
| + | [[Category: Svergun DI]] | ||
| + | [[Category: Van der Eijk H]] | ||
Current revision
apo-Trehalose transferase (apo-TreT) from Thermoproteus uzoniensis
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