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High-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase from -An Enzyme Involved in the Photosynthetic Calvin-Benson Cycle.

TitleHigh-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase from -An Enzyme Involved in the Photosynthetic Calvin-Benson Cycle.
Publication TypeJournal Article
Year of Publication2020
AuthorsLe Moigne, T, Crozet, P, Lemaire, SD, Henri, J
JournalInt J Mol Sci
Volume21
Issue20
Date Published2020 Oct 21
ISSN1422-0067
Abstract

The Calvin-Benson cycle is the key metabolic pathway of photosynthesis responsible for carbon fixation and relies on eleven conserved enzymes. Ribose-5-phosphate isomerase (RPI) isomerizes ribose-5-phosphate into ribulose-5-phosphate and contributes to the regeneration of the Rubisco substrate. Plant RPI is the target of diverse post-translational modifications including phosphorylation and thiol-based modifications to presumably adjust its activity to the photosynthetic electron flow. Here, we describe the first experimental structure of a photosynthetic RPI at 1.4 Å resolution. Our structure confirms the composition of the catalytic pocket of the enzyme. We describe the homo-dimeric state of the protein that we observed in the crystal and in solution. We also map the positions of previously reported post-translational modifications and propose mechanisms by which they may impact the catalytic parameters. The structural data will inform the biochemical modeling of photosynthesis.

DOI10.3390/ijms21207787
Alternate JournalInt J Mol Sci
PubMed ID33096784
PubMed Central IDPMC7589169
Grant List19-CE11-0009-01 / / Agence Nationale de la Recherche /
11-LABX-0011 / / Agence Nationale de la Recherche /