4IOT
High-resolution Structure of Triosephosphate isomerase from E. coli
Summary for 4IOT
| Entry DOI | 10.2210/pdb4iot/pdb |
| Descriptor | Triosephosphate isomerase, SULFATE ION (3 entities in total) |
| Functional Keywords | structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, tim barrel, conversion of dihydroxyacetone phosphate to d-glyceraldehyde-3-phosphate, cytosol, isomerase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm (By similarity): B1XB85 |
| Total number of polymer chains | 2 |
| Total formula weight | 54103.67 |
| Authors | Vinaik, R.,Kozlov, G.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2013-01-08, release date: 2013-01-23, Last modification date: 2023-09-20) |
| Primary citation | 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, 69:499-502, 2013 Cited by PubMed Abstract: 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 Å resolution, which is a significant improvement over the previous structure. PubMed: 23695562DOI: 10.1107/S1744309113010841 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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