2P3V

Thermotoga maritima IMPase TM1415

2P3V の概要

• エントリーDOI: 10.2210/pdb2p3v/pdb
• 関連するPDBエントリー: 2P3N
• 分子名称: Inositol-1-monophosphatase, S,R MESO-TARTARIC ACID (3 entities in total)
• 機能のキーワード: inositol, phosphatase, asymmetric tetramer, hydrolase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 115331.16

構造登録者

Stieglitz, K.A.,Roberts, M.F.,Li, W.,Stec, B. (登録日: 2007-03-09, 公開日: 2007-04-24, 最終更新日: 2024-08-07)

主引用文献

Stieglitz, K.A.,Roberts, M.F.,Li, W.,Stec, B.
Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima.
Febs J., 274:2461-2469, 2007

PubMed Abstract: The structure of the first tetrameric inositol monophosphatase (IMPase) has been solved. This enzyme, from the eubacterium Thermotoga maritima, similarly to its archaeal homologs exhibits dual specificity with both IMPase and fructose-1,6-bisphosphatase activities. The tetrameric structure of this unregulated enzyme is similar, in its quaternary assembly, to the allosterically regulated tetramer of fructose-1,6-bisphosphatase. The individual dimers are similar to the human IMPase. Additionally, the structures of two crystal forms of IMPase show significant differences. In the first crystal form, the tetrameric structure is symmetrical, with the active site loop in each subunit folded into a beta-hairpin conformation. The second form is asymmetrical and shows an unusual structural change. Two of the subunits have the active site loop folded into a beta-hairpin structure, whereas in the remaining two subunits the same loop adopts an alpha-helical conformation.

PubMed: 17419729
DOI: 10.1111/j.0014-2956.2007.05779.x

実験手法

X-RAY DIFFRACTION (2.4 Å)