2xa2: Difference between revisions
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<StructureSection load='2xa2' size='340' side='right' caption='[[2xa2]], [[Resolution|resolution]] 2.50Å' scene=''> | ==Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG== | ||
<StructureSection load='2xa2' size='340' side='right'caption='[[2xa2]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xa2]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2xa2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XA2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xa2 OCA], [https://pdbe.org/2xa2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xa2 RCSB], [https://www.ebi.ac.uk/pdbsum/2xa2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xa2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRET_PYRHO TRET_PYRHO] Synthesizes trehalose from ADP-, UDP- or GDP-glucose and glucose.<ref>PMID:15737605</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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 2xa2" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Jung | [[Category: Jung T-Y]] | ||
[[Category: Lee | [[Category: Lee S-B]] | ||
[[Category: Lim | [[Category: Lim M-Y]] | ||
[[Category: Song | [[Category: Song H-N]] | ||
[[Category: Woo | [[Category: Woo E-J]] | ||
[[Category: Yoon | [[Category: Yoon S-M]] | ||
Latest revision as of 15:45, 17 January 2024
Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPGCrystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG
Structural highlights
FunctionTRET_PYRHO Synthesizes trehalose from ADP-, UDP- or GDP-glucose and glucose.[1] Publication Abstract from PubMedMany microorganisms produce trehalose for stability and survival against various environmental stresses. Unlike the widely distributed trehalose-biosynthetic pathway, which utilizes uridine diphosphate glucose and glucose-6-phosphate, the newly identified enzyme trehalose glycosyltransferring synthase (TreT) from hyperthermophilic bacteria and archaea synthesizes an alpha,alpha-trehalose from nucleoside diphosphate glucose and glucose. In the present study, we determined the crystal structure of TreT from Pyrococcus horikoshii at 2.3 A resolution to understand the detailed mechanism of this novel trehalose synthase. The conservation of essential residues in TreT and the high overall structural similarity of the N-terminal domain to that of trehalose phosphate synthase (TPS) imply that the catalytic reaction of TreT for trehalose synthesis would follow a similar mechanism to that of TPS. The acceptor binding site of TreT shows a wide and commodious groove and lacks the long flexible loop that plays a gating role in ligand binding in TPS. The observation of a wide space at the fissure between two domains and the relative shift of the N-domain in one of the crystal forms suggest that an interactive conformational change between two domains would occur, allowing a more compact architecture for catalysis. The structural analysis and biochemical data in this study provide a molecular basis for understanding the synthetic mechanism of trehalose, or the nucleotide sugar in reverse reaction of the TreT, in extremophiles that may have important industrial implications. Structural Insights on the New Mechanism of Trehalose Synthesis by Trehalose Synthase TreT from Pyrococcus horikoshii.,Woo EJ, Ryu SI, Song HN, Jung TY, Yeon SM, Lee HA, Park BC, Park KH, Lee SB J Mol Biol. 2010 Oct 1. PMID:20888836[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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