5B3F

Crystal structure of phosphoribulokinase from Methanospirillum hungatei

5B3F の概要

• エントリーDOI: 10.2210/pdb5b3f/pdb
• 分子名称: Phosphoribulokinase/uridine kinase, SULFATE ION (3 entities in total)
• 機能のキーワード: archaea, kinase, transferase
• 由来する生物種: Methanospirillum hungatei JF-1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79744.03

構造登録者

Matsumura, H.,Ashida, H. (登録日: 2016-02-22, 公開日: 2017-01-18, 最終更新日: 2024-11-06)

主引用文献

Kono, T.,Mehrotra, S.,Endo, C.,Kizu, N.,Matusda, M.,Kimura, H.,Mizohata, E.,Inoue, T.,Hasunuma, T.,Yokota, A.,Matsumura, H.,Ashida, H.
A RuBisCO-mediated carbon metabolic pathway in methanogenic archaea
Nat Commun, 8:14007-14007, 2017

PubMed Abstract: Two enzymes are considered to be unique to the photosynthetic Calvin-Benson cycle: ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), responsible for CO fixation, and phosphoribulokinase (PRK). Some archaea possess bona fide RuBisCOs, despite not being photosynthetic organisms, but are thought to lack PRK. Here we demonstrate the existence in methanogenic archaea of a carbon metabolic pathway involving RuBisCO and PRK, which we term 'reductive hexulose-phosphate' (RHP) pathway. These archaea possess both RuBisCO and a catalytically active PRK whose crystal structure resembles that of photosynthetic bacterial PRK. Capillary electrophoresis-mass spectrometric analysis of metabolites reveals that the RHP pathway, which differs from the Calvin-Benson cycle only in a few steps, is active in vivo. Our work highlights evolutionary and functional links between RuBisCO-mediated carbon metabolic pathways in methanogenic archaea and photosynthetic organisms. Whether the RHP pathway allows for autotrophy (that is, growth exclusively with CO as carbon source) remains unknown.

PubMed: 28082747
DOI: 10.1038/ncomms14007

実験手法

X-RAY DIFFRACTION (2.5 Å)