4wf7: Difference between revisions
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==Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis== | ==Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis== | ||
<StructureSection load='4wf7' size='340' side='right' caption='[[4wf7]], [[Resolution|resolution]] 2.21Å' scene=''> | <StructureSection load='4wf7' size='340' side='right' caption='[[4wf7]], [[Resolution|resolution]] 2.21Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tvu|4tvu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tvu|4tvu]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maltose_alpha-D-glucosyltransferase Maltose alpha-D-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.16 5.4.99.16] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maltose_alpha-D-glucosyltransferase Maltose alpha-D-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.16 5.4.99.16] </span></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=4wf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wf7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wf7 RCSB], [http://www.ebi.ac.uk/pdbsum/4wf7 PDBsum]</span></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=4wf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wf7 OCA], [http://pdbe.org/4wf7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wf7 RCSB], [http://www.ebi.ac.uk/pdbsum/4wf7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wf7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4wf7" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 17:30, 5 August 2016
Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysisCrystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis
Structural highlights
Publication Abstract from PubMedTrehalose synthase catalyzes the simple conversion of the inexpensive maltose into trehalose with a side reaction of hydrolysis. Here, the crystal structures of the wild type and the N253A mutant of Deinococcus radiodurans trehalose synthase (DrTS) in complex with the inhibitor Tris are reported. DrTS consists of a catalytic (beta/alpha)8 barrel, subdomain B, a C-terminal beta domain and two TS-unique subdomains (S7 and S8). The C-terminal domain and S8 contribute the majority of the dimeric interface. DrTS shares high structural homology with sucrose hydrolase, amylosucrase and sucrose isomerase in complex with sucrose, in particular a virtually identical active-site architecture and a similar substrate-induced rotation of subdomain B. The inhibitor Tris was bound and mimics a sugar at the -1 subsite. A maltose was modelled into the active site, and subsequent mutational analysis suggested that Tyr213, Glu320 and Glu324 are essential within the +1 subsite for the TS activity. In addition, the interaction networks between subdomains B and S7 seal the active-site entrance. Disruption of such networks through the replacement of Arg148 and Asn253 with alanine resulted in a decrease in isomerase activity by 8-9-fold and an increased hydrolase activity by 1.5-1.8-fold. The N253A structure showed a small pore created for water entry. Therefore, our DrTS-Tris may represent a substrate-induced closed conformation that will facilitate intramolecular isomerization and minimize disaccharide hydrolysis. Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization.,Wang YL, Chow SY, Lin YT, Hsieh YC, Lee GC, Liaw SH Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3144-54. doi:, 10.1107/S1399004714022500. Epub 2014 Nov 22. PMID:25478833[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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