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4iot

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Revision as of 21:00, 16 November 2022 by OCA (Talk | contribs)

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High-resolution Structure of Triosephosphate isomerase from E. coli

Structural highlights

4iot is a 2 chain structure with sequence from Escherichia coli str. K-12 substr. DH10B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPIS_ECODH

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kozlov G, Vinaik R, Gehring K. Triosephosphate isomerase is a common crystallization contaminant of soluble His-tagged proteins produced in Escherichia coli. 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 doi:10.1107/S1744309113010841