ArticleThe Journal of biological chemistry2012
Rigid core and flexible terminus: structure of solubilized light-harvesting chlorophyll a/b complex (LHCII) measured by EPR.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Electron Paramagnetic Resonance Spectroscopy of Spin-Labeled Lipids for Studying Lipid-Protein Interaction in Model and Biomembranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The origin of pigment-binding differences in CP29 and LHCII: the role of protein structure and dynamics.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Plant LHC-like proteins show robust folding and static non-photochemical quenching.Nature communications · 2021Article
- Uncovering the interactions driving carotenoid binding in light-harvesting complexes.Chemical science · 2021Article
- Lipid and protein dynamics of stacked and cation-depletion induced unstacked thylakoid membranes.BBA advances · 2021Article
- Viewing rare conformations of the βProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dynamical and allosteric regulation of photoprotection in light harvesting complex II.Science China. Chemistry · 2020Article
- Molecular dynamics simulations in photosynthesis.Photosynthesis research · 2020Review
- A proteoliposome-based system reveals how lipids control photosynthetic light harvesting.The Journal of biological chemistry · 2020Article
- The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018Article
- MMM: A toolbox for integrative structure modeling.Protein science : a publication of the Protein Society · 2018Article
- A pathway for protective quenching in antenna proteins of Photosystem II.Scientific reports · 2017Article
- Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN(-) binding defined by EPR-based hybrid method.Scientific reports · 2016Article
- Modeling of the N-terminal Section and the Lumenal Loop of Trimeric Light Harvesting Complex II (LHCII) by Using EPR.The Journal of biological chemistry · 2015Article
- From light-harvesting to photoprotection: structural basis of the dynamic switch of the major antenna complex of plants (LHCII).Scientific reports · 2015Article
- Membrane crystals of plant light-harvesting complex II disassemble reversibly in light.Plant & cell physiology · 2014Article
- Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Probing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance.Biophysical journal · 2014Article
- Insights into the photoprotective switch of the major light-harvesting complex II (LHCII): a preserved core of arginine-glutamate interlocked helices complemented by adjustable loops.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure of the major light-harvesting chlorophyll a/b complex (LHCII) was analyzed by pulsed EPR measurements and compared with the crystal structure. Site-specific spin labeling of the recombinant protein allowed the measurement of distance distributions over several intra- and intermolecular distances in monomeric and trimeric LHCII, yielding information on the protein structure and its local flexibility. A spin label rotamer library based on a molecular dynamics simulation was used to take the local mobility of spin labels into account. The core of LHCII in solution adopts a structure very similar or identical to the one seen in crystallized LHCII trimers with little motional freedom as indicated by narrow distance distributions along and between α helices. However, distances comprising the lumenal loop domain show broader distance distributions, indicating some mobility of this loop structure. Positions in the hydrophilic N-terminal domain, upstream of the first trans-membrane α helix, exhibit more and more mobility the closer they are to the N terminus. The nine amino acids at the very N terminus that have not been resolved in any of the crystal structure analyses give rise to very broad and possibly bimodal distance distributions, which may represent two families of preferred conformations.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.