Maes, Dominique and Zeelen, Johan P. and Thanki, Narmada and Beaucamp, Nicola and Alvarez, Marco and Thi, Minh Hoa Dao and Backmann, Jan and Martial, Joseph A. and Wyns, Lode and Jaenicke, Rainer and Wierenga, Rik K. (1999) The crystal structure of triosephosphate isomerase (TIM) from Thermtotoga maritima: A comparative thermostability structural analysis of ten different TIM structures. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 37 (3). pp. 441-453. ISSN 0887-3585,
Full text not available from this repository. (Request a copy)Abstract
The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM), The enzyme is a tetramer, assembled as a dimer of dimers, suggesting that the tetrameric wild-type phosphoglycerate kinase PGK-TIM fusion protein consists of a core of two TIM dimers covalently linked to 4 PGK units. The crystal structure of TmTIM represents the most thermostable TIM presently known in its SD-structure, It adds to a series of nine known TIM structures from a wide variety of organisms, spanning the range from psychrophiles to hyperthermophiles, Several properties believed to be involved in the adaptation to different temperatures were calculated and compared for all ten structures. No sequence preferences, correlated with thermal stability, were apparent from the amino acid composition or from the analysis of the loops and secondary structure elements of the ten TIMs, A common feature for both psychrophilic and T. maritima TIM is the large number of salt bridges compared with the number found in mesophilic TIMs. In the two thermophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process. Proteins 1999;37:441-453. (C) 1999 Wiley-Liss, Inc.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BACTERIUM THERMOTOGA-MARITIMA; ENHANCED PROTEIN THERMOSTABILITY; ANGSTROM RESOLUTION; ALPHA-HELICES; DRUG DESIGN; KEY ROLE; ENZYME; STABILITY; STABILIZATION; YEAST; hydrophobicity; hyperthermophile; psychrophile; salt bridges; thermophile |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 13 Dec 2022 06:29 |
| Last Modified: | 13 Dec 2022 06:29 |
| URI: | https://pred.uni-regensburg.de/id/eprint/48842 |
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