1tre
From Proteopedia
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THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION
Overview
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.
About this Structure
1TRE is a Single protein structure of sequence from Escherichia coli. Active as Triose-phosphate isomerase, with EC number 5.3.1.1 Full crystallographic information is available from OCA.
Reference
Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution., Noble ME, Zeelen JP, Wierenga RK, Mainfroid V, Goraj K, Gohimont AC, Martial JA, Acta Crystallogr D Biol Crystallogr. 1993 Jul 1;49(Pt 4):403-17. PMID:15299515
Page seeded by OCA on Wed Nov 21 03:32:03 2007
