2B2K

structure of Y104F IDI-1 mutant in complex with EIPP

2B2K の概要

• エントリーDOI: 10.2210/pdb2b2k/pdb
• 関連するPDBエントリー: 1HX3
• 分子名称: Isopentenyl-diphosphate delta-isomerase, MANGANESE (II) ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: complex, isomerase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: Q46822
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41943.48

構造登録者

Wouters, J. (登録日: 2005-09-19, 公開日: 2006-09-05, 最終更新日: 2024-10-23)

主引用文献

de Ruyck, J.,Durisotti, V.,Oudjama, Y.,Wouters, J.
Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography
J.Biol.Chem., 281:17864-17869, 2006

PubMed Abstract: Isopentenyl-diphosphate (IPP):dimethylallyl diphosphate isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate, but identity of the acidic moiety providing the proton is still not clear. Multiple sequence alignments and geometrical features observed in crystal structures of complexes with IPP isomerase suggest that Tyr-104 could play an important role during catalysis. A series of mutants was constructed by directed mutagenesis and characterized by enzymology. Crystallographic and thermal denaturation data for Y104A and Y104F mutants were obtained. Those data demonstrate the importance of residue Tyr-104 for proper folding of Escherichia coli type I IPP isomerase.

PubMed: 16617181
DOI: 10.1074/jbc.M601851200

実験手法

X-RAY DIFFRACTION (1.97 Å)