5B3F
Crystal structure of phosphoribulokinase from Methanospirillum hungatei
Summary for 5B3F
Entry DOI | 10.2210/pdb5b3f/pdb |
Descriptor | Phosphoribulokinase/uridine kinase, SULFATE ION (3 entities in total) |
Functional Keywords | archaea, kinase, transferase |
Biological source | Methanospirillum hungatei JF-1 |
Total number of polymer chains | 2 |
Total formula weight | 79744.03 |
Authors | Matsumura, H.,Ashida, H. (deposition date: 2016-02-22, release date: 2017-01-18, Last modification date: 2024-11-06) |
Primary citation | 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 Cited by 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: 28082747DOI: 10.1038/ncomms14007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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