Structural basis of diadinoxanthin-Chl a/b-binding proteins in the photosystem I supercomplex of <i>Euglena gracilis</i>.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 41790873.
- Also identified by DOI 10.1126/sciadv.aea5561 and PMC identifier 12965295.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
<i>Euglena gracilis</i> is a phototrophic flagellate that has evolved through secondary endosymbiotic events and belongs to green-lineage organisms. We report a unique structure of photosystem I-light harvesting complex I (PSI-LHCI) supercomplex from <i>E. gracilis</i> at a 2.23-angstrom resolution by cryo-electron microscopy. The supercomplex is composed of 8 core subunits and 16 LHCIs and exhibits distinctive structural features compared to its counterparts in green algae and plants. The LHCI subunits encircle the core complex, forming a two-layered arrangement that comprises six pairs of tightly packed heterodimers. Specifically, the 16 LHCIs consist of 4 diadinoxanthin-chlorophyll (Chl) a/b-binding antennae (Lhcbm) and 12 diadinoxanthin-Chl a-binding antennae (Lhca), and they exhibit characteristic pigment compositions combining features of green- and red-lineage organisms. These findings provide a robust structural foundation for elucidating the mechanisms of light harvesting and energy transfer as well as insights into the evolutionary changes of green-lineage PSI-LHCI.
Medical subject headings
- Photosystem I Protein Complex
- Euglena gracilis
- Xanthophylls
- Light-Harvesting Protein Complexes
- Chlorophyll Binding Proteins
- Chlorophyll