Structure of a green algal photosystem I in complex with a large number of light-harvesting complex I subunits.

Nat Plants

State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.

Published: March 2019

Photosystem I (PSI) is a highly efficient natural light-energy converter, and has diverse light-harvesting antennas associated with its core in different photosynthetic organisms. In green algae, an extremely large light-harvesting complex I (LHCI) captures and transfers energy to the PSI core. Here, we report the structure of PSI-LHCI from a green alga Bryopsis corticulans at 3.49 Å resolution, obtained by single-particle cryo-electron microscopy, which revealed 13 core subunits including subunits characteristic of both prokaryotes and eukaryotes, and 10 light-harvesting complex a (Lhca) antennas that form a double semi-ring and an additional Lhca dimer, including a novel four-transmembrane-helix Lhca. In total, 244 chlorophylls were identified, some of which were located at key positions for the fast energy transfer. These results provide a firm structural basis for unravelling the mechanisms of light-energy harvesting, transfer and quenching in the green algal PSI-LHCI, and important clues as to how PSI-LHCI has changed during evolution.

Download full-text PDF

Source
http://dx.doi.org/10.1038/s41477-019-0379-yDOI Listing

Publication Analysis

Top Keywords

light-harvesting complex
12
green algal
8
structure green
4
algal photosystem
4
complex
4
photosystem complex
4
complex large
4
large number
4
light-harvesting
4
number light-harvesting
4

Similar Publications

Many important processes in cells depend on the transfer of protons through water wires embedded in transmembrane proteins. Herein, we have performed more than 55 μs all-atom simulations of the light-harvesting complex of a diatom, i.e.

View Article and Find Full Text PDF

Probing the Dual Role of Ca in the LH1-RC Complex by Constructing and Analyzing Ca-Bound and Ca-Free LH1 Complexes.

Biomolecules

January 2025

Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.

The genome of the mildly thermophilic hot spring purple sulfur bacterium, (.) , contains a multigene family that encodes a series of α- and β-polypeptides, collectively forming a heterogeneous light-harvesting 1 (LH1) complex. The LH1, therefore, offers a unique model for studying an intermediate phenotype between phototrophic thermophilic and mesophilic bacteria, particularly regarding their LH1 transition and moderately enhanced thermal stability.

View Article and Find Full Text PDF

Photosynthesis, which is the foundation of crop growth and development, is accompanied by complex transcriptional regulatory mechanisms. Research has established that brassinosteroids (BRs) play a role in regulating plant photosynthesis, with the majority of research focusing on the physiological level and regulation of rate-limiting enzymes in the dark reactions of photosynthesis. However, studies on their effects on maize photosynthesis, specifically on light-harvesting antenna proteins, have yet to be conducted.

View Article and Find Full Text PDF

Photosynthetic organisms rely on a network of light-harvesting protein-pigment complexes to efficiently absorb sunlight and transfer excitation energy to reaction centre proteins where charge separation occurs. In photosynthetic purple bacteria, these complexes are embedded within the cell membrane, with lipid composition affecting complex clustering, thereby impacting inter-complex energy transfer. However, the impact of the lipid bilayer on intra-complex excitation dynamics is less understood.

View Article and Find Full Text PDF

Molecular glue for phycobilisome attachment to photosystem II in sp. PCC 7002.

Proc Natl Acad Sci U S A

January 2025

State Key Laboratory of Protein and Plant Genetic Engineering, School of Life Science, Peking University, Beijing 100871, People's Republic of China.

Phycobilisomes (PBS) are the major photosynthetic light-harvesting complexes in cyanobacteria and red algae. While the structures of PBS have been determined in atomic resolutions, how PBS are attached to the reaction centers of photosystems remains less clear. Here, we report that a linker protein (LcpA) is required for the attachment of PBS to photosystem II (PSII) in the cyanobacterium sp.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!