## Interactions Determining the Structural Integrity of the Trimer of Plant Light Harvesting Complex in Lipid Membranes

2021
Saini, Renu
Debnath, Ananya
Journal article
Published
##### Published in
The Journal of Membrane Biology ; 254 (2021), 2. - pp. 157-173. - Springer. - ISSN 0022-2631. - eISSN 1432-1424
##### Abstract
The structural basis for the stability of the trimeric form of the light harvesting complex (LHCII), a pigmented protein from green plants pivotal for photosynthesis, remains elusive till date. The protein embedded in a dipalmitoylphosphatidylcholine (DPPC) lipid membrane is investigated using all-atom molecular dynamics simulations to find out the interactions responsible for the structural integrity of the trimer and its relation to antenna function. Central association of chlorophyll a (CLA) molecules near the LHCII chains is attributed to a conserved coordination between the Mg of CLA and the oxygen of a specific residue of the first helix of a chain. The residue forms a salt-bridge with the fourth helix of the same chain of the trimer, not of the monomer. In an earlier experiment, three residues (WYR) at each chain of the trimer have been found indispensable for the trimerization and referred to as trimerization motif. We find that the residues of the trimerization motif are connected to the lipids or pigments by a chain of interactions rather than a direct contact. Synergistic effects of sequentially located hydrogen bonds and salt-bridges within monomers of the trimer keep the trimer conformation stable in association with the pigments or the lipids. These interactions are exclusively present in the pigmented trimer and not present in the monomer or in the unpigmented trimer. Thus, our results provide a molecular basis for the inherent stability of the LHCII trimer in a lipid membrane and explain many pre-existing experimental data.
540 Chemistry
##### Cite This
ISO 690SAINI, Renu, Christoph GLOBISCH, Leon FRANKE, Christine PETER, Ananya DEBNATH, 2021. Interactions Determining the Structural Integrity of the Trimer of Plant Light Harvesting Complex in Lipid Membranes. In: The Journal of Membrane Biology. Springer. 254(2), pp. 157-173. ISSN 0022-2631. eISSN 1432-1424. Available under: doi: 10.1007/s00232-020-00162-x
BibTex
@article{Saini2021-04Inter-52686,
year={2021},
doi={10.1007/s00232-020-00162-x},
title={Interactions Determining the Structural Integrity of the Trimer of Plant Light Harvesting Complex in Lipid Membranes},
number={2},
volume={254},
issn={0022-2631},
journal={The Journal of Membrane Biology},
pages={157--173},
author={Saini, Renu and Globisch, Christoph and Franke, Leon and Peter, Christine and Debnath, Ananya}
}

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<dcterms:abstract xml:lang="eng">The structural basis for the stability of the trimeric form of the light harvesting complex (LHCII), a pigmented protein from green plants pivotal for photosynthesis, remains elusive till date. The protein embedded in a dipalmitoylphosphatidylcholine (DPPC) lipid membrane is investigated using all-atom molecular dynamics simulations to find out the interactions responsible for the structural integrity of the trimer and its relation to antenna function. Central association of chlorophyll a (CLA) molecules near the LHCII chains is attributed to a conserved coordination between the Mg of CLA and the oxygen of a specific residue of the first helix of a chain. The residue forms a salt-bridge with the fourth helix of the same chain of the trimer, not of the monomer. In an earlier experiment, three residues (WYR) at each chain of the trimer have been found indispensable for the trimerization and referred to as trimerization motif. We find that the residues of the trimerization motif are connected to the lipids or pigments by a chain of interactions rather than a direct contact. Synergistic effects of sequentially located hydrogen bonds and salt-bridges within monomers of the trimer keep the trimer conformation stable in association with the pigments or the lipids. These interactions are exclusively present in the pigmented trimer and not present in the monomer or in the unpigmented trimer. Thus, our results provide a molecular basis for the inherent stability of the LHCII trimer in a lipid membrane and explain many pre-existing experimental data.</dcterms:abstract>
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