2wtx
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2wtx is ON HOLD until sometime in the future Authors: Errey, J.C., Lee, S.S., Gibson, R.P., Martinez-Fleites, C., Barry, C.S., Jung, P.M.J., OSulliv...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase== | |
| - | + | <StructureSection load='2wtx' size='340' side='right'caption='[[2wtx]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2wtx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WTX 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]] 2.2Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=VDO:[(1R,2R,3S,4S,5S)-2,3,4-TRIHYDROXY-5-{[(1S,4R,5S,6S)-4,5,6-TRIHYDROXY-3-(HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}CYCLOHEXYL]METHYL+DIHYDROGEN+PHOSPHATE'>VDO</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=2wtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wtx OCA], [https://pdbe.org/2wtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wtx RCSB], [https://www.ebi.ac.uk/pdbsum/2wtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wtx ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OTSA_ECOLI OTSA_ECOLI] Catalyzes the transfer of glucose from UDP-glucose to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. Essential for viability of the cells at low temperatures and at elevated osmotic strength.<ref>PMID:1310094</ref> <ref>PMID:3131312</ref> <ref>PMID:12105274</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wt/2wtx_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wtx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Barry CS]] | ||
| + | [[Category: Davies GJ]] | ||
| + | [[Category: Davis BG]] | ||
| + | [[Category: Errey JC]] | ||
| + | [[Category: Gibson RP]] | ||
| + | [[Category: Jung PMJ]] | ||
| + | [[Category: Lee SS]] | ||
| + | [[Category: Martinez-Fleites C]] | ||
| + | [[Category: OSullivan A]] | ||
Current revision
Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase
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