5HZ2

Crystal structure of PhaC1 from Ralstonia eutropha

5HZ2 の概要

• エントリーDOI: 10.2210/pdb5hz2/pdb
• 分子名称: Poly-beta-hydroxybutyrate polymerase, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Cupriavidus necator
• 細胞内の位置: Cytoplasm: P23608
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44507.02

構造登録者

Kim, J.,Kim, K.-J. (登録日: 2016-02-02, 公開日: 2016-12-07, 最終更新日: 2017-04-05)

主引用文献

Kim, J.,Kim, Y.J.,Choi, S.Y.,Lee, S.Y.,Kim, K.J.
Crystal structure of Ralstonia eutropha polyhydroxyalkanoate synthase C-terminal domain and reaction mechanisms.
Biotechnol J, 12:-, 2017

PubMed Abstract: Polyhydroxyalkanoates (PHAs) are natural polyesters synthesized by numerous microorganisms as energy and reducing power storage materials, and have attracted much attention as substitutes for petroleum-based plastics. Here, we report the first crystal structure of Ralstonia eutropha PHA synthase at 1.8 Å resolution and structure-based mechanisms for PHA polymerization. RePhaC1 contains two distinct domains, the N-terminal (RePhaC1 ) and C-terminal domains (RePhaC1 ), and exists as a dimer. RePhaC1 catalyzes polymerization via non-processive ping-pong mechanism using a Cys-His-Asp catalytic triad. Molecular docking simulation of 3-hydroxybutyryl-CoA to the active site of RePhaC1 reveals residues involved in the formation of 3-hydroxybutyryl-CoA binding pocket and substrate binding tunnel. Comparative analysis with other polymerases elucidates how different classes of PHA synthases show different substrate specificities. Furthermore, we attempted structure-based protein engineering and developed a RePhaC1 mutant with enhanced PHA synthase activity.

PubMed: 27808482
DOI: 10.1002/biot.201600648

実験手法

X-RAY DIFFRACTION (1.8 Å)