6J7C

Crystal structure of proline racemase-like protein from Thermococcus litoralis in complex with proline

6J7C の概要

• エントリーDOI: 10.2210/pdb6j7c/pdb
• 分子名称: Proline racemase, PROLINE (3 entities in total)
• 機能のキーワード: proline racemase, hydroxyproline 2-epimerase, hyperthermophilic archaea, isomerase
• 由来する生物種: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38316.75

構造登録者

Watanabe, Y.,Watanabe, S.,Itoh, Y.,Watanabe, Y. (登録日: 2019-01-17, 公開日: 2019-02-27, 最終更新日: 2023-11-22)

主引用文献

Watanabe, Y.,Watanabe, S.,Itoh, Y.,Watanabe, Y.
Crystal structure of substrate-bound bifunctional proline racemase/hydroxyproline epimerase from a hyperthermophilic archaeon.
Biochem. Biophys. Res. Commun., 511:135-140, 2019

PubMed Abstract: The hypothetical OCC_00372 protein from Thermococcus litoralis is a member of the ProR superfamily from hyperthermophilic archaea and exhibits unique bifunctional proline racemase/hydroxyproline 2-epimerase activity. However, the molecular mechanism of the broad substrate specificity and extreme thermostability of this enzyme (TlProR) remains unclear. Here we determined the crystal structure of TlProR at 2.7 Å resolution. Of note, a substrate proline molecule, derived from expression host Escherichia coli cells, was tightly bound in the active site of TlProR. The substrate bound structure and mutational analyses suggested that Trp241 is involved in hydroxyproline recognition by making a hydrogen bond between the indole group of Trp241 and the hydroxyl group of hydroxyproline. Additionally, Tyr171 may contribute to the thermostability by making hydrogen bonds between the hydroxyl group of Tyr171 and catalytic residues. Our structural and functional analyses provide a structural basis for understanding the molecular mechanism of substrate specificity and thermostability of ProR superfamily proteins.

PubMed: 30773259
DOI: 10.1016/j.bbrc.2019.01.141

実験手法

X-RAY DIFFRACTION (2.7 Å)