4IOT

High-resolution Structure of Triosephosphate isomerase from E. coli

4IOT の概要

• エントリーDOI: 10.2210/pdb4iot/pdb
• 分子名称: Triosephosphate isomerase, SULFATE ION (3 entities in total)
• 機能のキーワード: structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, tim barrel, conversion of dihydroxyacetone phosphate to d-glyceraldehyde-3-phosphate, cytosol, isomerase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (By similarity): B1XB85
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54103.67

構造登録者

Vinaik, R.,Kozlov, G.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2013-01-08, 公開日: 2013-01-23, 最終更新日: 2023-09-20)

主引用文献

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

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: 23695562
DOI: 10.1107/S1744309113010841

実験手法

X-RAY DIFFRACTION (1.85 Å)