1B9B

TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA

1B9B の概要

• エントリーDOI: 10.2210/pdb1b9b/pdb
• 分子名称: PROTEIN (TRIOSEPHOSPHATE ISOMERASE), SULFATE ION (3 entities in total)
• 機能のキーワード: isomerase, thermophilic, thermotoga maritima
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cytoplasm: P36204
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57300.22

構造登録者

Maes, D.,Wierenga, R.K. (登録日: 1999-02-09, 公開日: 2000-01-01, 最終更新日: 2024-10-16)

主引用文献

Maes, D.,Zeelen, J.P.,Thanki, N.,Beaucamp, N.,Alvarez, M.,Thi, M.H.,Backmann, J.,Martial, J.A.,Wyns, L.,Jaenicke, R.,Wierenga, R.K.
The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
Proteins, 37:441-453, 1999

PubMed 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 3D-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.

PubMed: 10591103
DOI: 10.1002/(SICI)1097-0134(19991115)37:3<441::AID-PROT11>3.3.CO;2-Z

実験手法

X-RAY DIFFRACTION (2.85 Å)