2zvr
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2zvr is ON HOLD until Paper Publication Authors: Sakuraba, H., Ohshima, T. Description: Crystal structure of a D-tagatose 3-epimerase homologue fro...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a D-tagatose 3-epimerase-related protein from Thermotoga maritima== | |
| - | + | <StructureSection load='2zvr' size='340' side='right'caption='[[2zvr]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2zvr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZVR 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvr OCA], [https://pdbe.org/2zvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zvr RCSB], [https://www.ebi.ac.uk/pdbsum/2zvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvr ProSAT]</span></td></tr> | |
| - | '' | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IOLO_THEMA IOLO_THEMA] Catalyzes the reversible epimerization between 5-keto-L-gluconate (5-dehydro-L-gluconate) and D-tagaturonate, and thus probably functions in a myo-inositol degradation pathway together with IolG, IolM and IolN (PubMed:23441918). Is not active on the enantiomer 5-keto-D-gluconate (PubMed:23441918). Was also shown to be a nonphosphorylated sugar isomerase with broad substrate specificity in vitro (PubMed:28258150). Is able to catalyze the reversible C3-epimerization of L-ribulose to L-xylulose, D-ribulose to D-xylulose, D-psicose to D-fructose, and D-tagatose to D-sorbose, with a substrate preference for ketopentoses rather than ketohexoses (PubMed:28258150). Also catalyzes the aldose-ketose isomerization reaction from either D-erythrose or D-threose to D-erythrulose (PubMed:28258150). Exhibits no activity for C4-epimerization of D-tagatose to D-fructose (PubMed:28258150).<ref>PMID:23441918</ref> <ref>PMID:28258150</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/zv/2zvr_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=2zvr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima]] | ||
| + | [[Category: Ohshima T]] | ||
| + | [[Category: Sakuraba H]] | ||
Current revision
Crystal structure of a D-tagatose 3-epimerase-related protein from Thermotoga maritima
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