1TRE

THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION

1TRE の概要

• エントリーDOI: 10.2210/pdb1tre/pdb
• 分子名称: TRIOSEPHOSPHATE ISOMERASE (2 entities in total)
• 機能のキーワード: intramolecular oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54005.64

構造登録者

Noble, M.E.M.,Wierenga, R.K. (登録日: 1992-10-12, 公開日: 1993-10-31, 最終更新日: 2024-02-14)

主引用文献

Noble, M.E.,Zeelen, J.P.,Wierenga, R.K.,Mainfroid, V.,Goraj, K.,Gohimont, A.C.,Martial, J.A.
Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution.
Acta Crystallogr.,Sect.D, 49:403-417, 1993

PubMed Abstract: The structure of triosephosphate isomerase (TIM) from the organism Escherichia coli has been determined at a resolution of 2.6 A. The structure was solved by the molecular replacement method, first at 2.8 A resolution with a crystal grown by the technique of hanging-drop crystallization from a mother liquor containing the transition-state analogue 2-phosphoglycolate (2PG). As a search model in the molecular replacement calculations, the refined structure of TIM from Trypanosoma brucei, which has a sequence identity of 46% compared to the enzyme from E. coli, was used. An E. coli TIM crystal grown in the absence of 2PG, diffracting to 2.6 A resolution, was later obtained by application of the technique of macro-seeding using a seed crystal grown from a mother liquor without 2PG. The final 2.6 A model has a crystallographic R factor of 11.9%, and agrees well with standard stereochemical parameters. The structure of E. coli TIM suggests the importance of residues which favour helix initiation for the formation of the TIM fold. In addition, TIM from E. coli shows peculiarities in its dimer interface, and in the packing of core residues within the beta-barrel.

PubMed: 15299515
DOI: 10.1107/S0907444993002628

実験手法

X-RAY DIFFRACTION (2.6 Å)