4iot
From Proteopedia
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| - | + | ==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 [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IOT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=4iot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iot OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4iot RCSB], [http://www.ebi.ac.uk/pdbsum/4iot PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| + | |||
| + | ==See Also== | ||
| + | *[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Gehring, K | + | [[Category: Gehring, K]] |
| - | [[Category: Kozlov, G | + | [[Category: Kozlov, G]] |
| - | [[Category: Vinaik, R | + | [[Category: Vinaik, R]] |
[[Category: Bsgi]] | [[Category: Bsgi]] | ||
[[Category: Conversion of dihydroxyacetone phosphate to d-glyceraldehyde-3-phosphate]] | [[Category: Conversion of dihydroxyacetone phosphate to d-glyceraldehyde-3-phosphate]] | ||
[[Category: Cytosol]] | [[Category: Cytosol]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
| - | [[Category: Montreal-kingston bacterial structural genomics initiative]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
Revision as of 14:24, 4 January 2015
High-resolution Structure of Triosephosphate isomerase from E. coli
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