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Structural basis of metabolite transport by the chloroplast outer envelope channel OEP21.
Nat. Struct. Mol. Biol. 30, 761-769 (2023)
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DOI
PMC
Triose phosphates (TPs) are the primary products of photosynthetic CO2 fixation in chloroplasts, which need to be exported into the cytosol across the chloroplast inner envelope (IE) and outer envelope (OE) membranes to sustain plant growth. While transport across the IE is well understood, the mode of action of the transporters in the OE remains unclear. Here we present the high-resolution nuclear magnetic resonance (NMR) structure of the outer envelope protein 21 (OEP21) from garden pea, the main exit pore for TPs in C3 plants. OEP21 is a cone-shaped β-barrel pore with a highly positively charged interior that enables binding and translocation of negatively charged metabolites in a competitive manner, up to a size of ~1 kDa. ATP stabilizes the channel and keeps it in an open state. Despite the broad substrate selectivity of OEP21, these results suggest that control of metabolite transport across the OE might be possible.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Solute Channel; Protein Import; Nmr; Membrane; Reveals; Reconstruction; Software; Plastids; Gui
ISSN (print) / ISBN
1545-9993
e-ISSN
1545-9985
Zeitschrift
Nature Structural & Molecular Biology
Quellenangaben
Band: 30,
Heft: 6,
Seiten: 761-769
Verlag
Nature Publishing Group
Verlagsort
New York, NY
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)
Förderungen
Helmholtz Zentrum Muenchen -Deutsches Forschungszentrum fuer Gesundheit und Umwelt (GmbH)