1hg3
From Proteopedia
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CRYSTAL STRUCTURE OF TETRAMERIC TIM FROM PYROCOCCUS WOESEI.
Overview
Comparative structural studies on proteins derived from organisms with, growth optima ranging from 15 to 100 degrees C are beginning to shed light, on the mechanisms of protein thermoadaptation. One means of sustaining, hyperthermostability is for proteins to exist in higher oligomeric forms, than their mesophilic homologues. Triosephosphate isomerase (TIM) is one, of the most studied enzymes, whose fold represents one of nature's most, common protein architectures. Most TIMs are dimers of approximately 250, amino acid residues per monomer. Here, we report the 2.7 A resolution, crystal structure of the extremely thermostable TIM from Pyrococcus, woesei, a hyperthermophilic archaeon growing optimally at 100 degrees C, representing the first archaeal TIM structure. P. woesei TIM exists as ... [(full description)]
About this Structure
1HG3 is a [Single protein] structure of sequence from [Pyrococcus woesei] with 3PP as [ligand]. Active as [Isomerase], with EC number [5.3.1.1]. Structure known Active Sites: PP1, PP2, PP3, PP4, PP5, PP6, PP7 and PP8. Full crystallographic information is available from [OCA].
Reference
Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase., Walden H, Bell GS, Russell RJ, Siebers B, Hensel R, Taylor GL, J Mol Biol. 2001 Mar 2;306(4):745-57. PMID:11243785
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