4bce: Difference between revisions
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==crystal structure of Ttb-gly N282T mutant== | |||
<StructureSection load='4bce' size='340' side='right'caption='[[4bce]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bce]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BCE 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]] 2Å</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=4bce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bce OCA], [https://pdbe.org/4bce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bce RCSB], [https://www.ebi.ac.uk/pdbsum/4bce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bce ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q53W75_THET8 Q53W75_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A large number of retaining glycosidases catalyze both hydrolysis and transglycosylation reactions, but little is known about what determines the balance between these two activities (transglycosylation/hydrolysis ratio). We previously obtained by directed evolution the mutants F401S and N282T of Thermus thermophilus beta-glycosidase (Ttbeta-gly, glycoside hydrolase family 1 (GH1)), which display a higher transglycosylation/hydrolysis ratio than the wild-type enzyme. In order to find the cause of these activity modifications, and thereby set up a generic method for easily obtaining transglycosidases from glycosidases, we determined their X-ray structure. No major structural changes could be observed which could help to rationalize the mutagenesis of glycosidases into transglycosidases. However, as these mutations are highly conserved in GH1 beta-glycosidases and are located around the -1 site, we pursued the isolation of new transglycosidases by targeting highly conserved amino acids located around the active site. Thus, by single-point mutagenesis on Ttbeta-gly, we created four new mutants that exhibit improved synthetic activity, producing disaccharides in yields of 68-90% against only 36% when native Ttbeta-gly was used. As all of the chosen positions were well conserved among GH1 enzymes, this approach is most probably a general route to convert GH1 glycosidases into transglycosidases. | |||
Semi-rational approach for converting a GH1 beta-glycosidase into a beta-transglycosidase.,Teze D, Hendrickx J, Czjzek M, Ropartz D, Sanejouand YH, Tran V, Tellier C, Dion M Protein Eng Des Sel. 2014 Jan;27(1):13-9. doi: 10.1093/protein/gzt057. Epub 2013 , Nov 27. PMID:24287187<ref>PMID:24287187</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bce" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Czjzek M]] | |||
[[Category: Dion M]] | |||
[[Category: Leroux C]] | |||
[[Category: Roncza J]] | |||
[[Category: Tellier C]] | |||
[[Category: Teze D]] | |||
[[Category: Tran V]] | |||