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Open Access Green as soon as Postprint is submitted to ZB.
Structural basis of metabolite transport by the chloroplast outer envelope channel OEP21.
Nat. Struct. Mol. Biol. 30, 761-769 (2023)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Solute Channel; Protein Import; Nmr; Membrane; Reveals; Reconstruction; Software; Plastids; Gui
ISSN (print) / ISBN
1545-9993
e-ISSN
1545-9985
Quellenangaben
Volume: 30,
Issue: 6,
Pages: 761-769
Publisher
Nature Publishing Group
Publishing Place
New York, NY
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
Grants
Helmholtz Zentrum Muenchen -Deutsches Forschungszentrum fuer Gesundheit und Umwelt (GmbH)