3WDM

Crystal structure of 4-phosphopantoate-beta-alanine ligase from Thermococcus kodakarensis

3WDM の概要

• エントリーDOI: 10.2210/pdb3wdm/pdb
• 関連するPDBエントリー: 3WDK 3WDL
• 分子名称: 4-phosphopantoate--beta-alanine ligase, ADENOSINE (3 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: Thermococcus kodakarensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 120635.36

構造登録者

Kishimoto, A.,Kita, A.,Ishibashi, T.,Tomita, H.,Yokooji, Y.,Imanaka, T.,Atomi, H.,Miki, K. (登録日: 2013-06-19, 公開日: 2014-04-02, 最終更新日: 2024-03-20)

主引用文献

Kishimoto, A.,Kita, A.,Ishibashi, T.,Tomita, H.,Yokooji, Y.,Imanaka, T.,Atomi, H.,Miki, K.
Crystal structure of phosphopantothenate synthetase from Thermococcus kodakarensis
Proteins, 82:1924-1936, 2014

PubMed Abstract: Bacteria/eukaryotes share a common pathway for coenzyme A biosynthesis which involves two enzymes to convert pantoate to 4'-phosphopantothenate. These two enzymes are absent in almost all archaea. Recently, it was reported that two novel enzymes, pantoate kinase, and phosphopantothenate synthetase (PPS), are responsible for this conversion in archaea. Here, we report the crystal structure of PPS from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complexes with substrates, ATP, and ATP and 4-phosphopantoate. PPS forms an asymmetric homodimer, in which two monomers composing a dimer, deviated from the exact twofold symmetry, displaying 4°-13° distortion. The structural features are consistent with the mutagenesis data and the results of biochemical experiments previously reported. Based on these structures, we discuss the catalytic mechanism by which PPS produces phosphopantoyl adenylate, which is thought to be a reaction intermediate.

PubMed: 24638914
DOI: 10.1002/prot.24546

実験手法

X-RAY DIFFRACTION (2 Å)