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4iot
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==High-resolution Structure of Triosephosphate isomerase from E. coli== | |
| + | <StructureSection load='4iot' size='340' side='right'caption='[[4iot]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4iot]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._DH10B Escherichia coli str. K-12 substr. DH10B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IOT 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]] 1.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4iot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iot OCA], [https://pdbe.org/4iot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iot RCSB], [https://www.ebi.ac.uk/pdbsum/4iot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iot ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TPIS_ECODH TPIS_ECODH] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Attempts to crystallize several mammalian proteins overexpressed in Escherichia coli revealed a common contaminant, triosephosphate isomerase, a protein involved in glucose metabolism. Even with triosephosphate isomerase present in very small amounts, similarly shaped crystals appeared in the crystallization drops in a number of polyethylene glycol-containing conditions. All of the target proteins were His-tagged and their purification involved immobilized metal-affinity chromatography (IMAC), a step that was likely to lead to triosephosphate isomerase contamination. Analysis of the triosephosphate isomerase crystals led to the structure of E. coli triosephosphate isomerase at 1.85 A resolution, which is a significant improvement over the previous structure. | ||
| - | + | Triosephosphate isomerase is a common crystallization contaminant of soluble His-tagged proteins produced in Escherichia coli.,Kozlov G, Vinaik R, Gehring K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):499-502. doi:, 10.1107/S1744309113010841. Epub 2013 Apr 30. PMID:23695562<ref>PMID:23695562</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4iot" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli str. K-12 substr. DH10B]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gehring K]] | ||
| + | [[Category: Kozlov G]] | ||
| + | [[Category: Vinaik R]] | ||
Current revision
High-resolution Structure of Triosephosphate isomerase from E. coli
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