ArticleThe Journal of biological chemistry2015
Modeling of the N-terminal Section and the Lumenal Loop of Trimeric Light Harvesting Complex II (LHCII) by Using EPR.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025Review
- Comparative evaluation of spin-label modeling methods for protein structural studies.Biophysical journal · 2022Article
- Protein dynamics and lipid affinity of monomeric, zeaxanthin-binding LHCII in thylakoid membranes.Biophysical journal · 2022Article
- Neural network interpretation using descrambler groups.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Conformational Dynamics of Light-Harvesting Complex II in a Native Membrane Environment.Biophysical journal · 2021Article
- Photoprotective Role of Neoxanthin in Plants and Algae.Molecules (Basel, Switzerland) · 2020Review
- Lipid Fingerprints and Cofactor Dynamics of Light-Harvesting Complex II in Different Membranes.Biophysical journal · 2019Article
- Deep neural network processing of DEER data.Science advances · 2018Article
- 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
- 9-cis-Neoxanthin in Light Harvesting Complexes of Photosystem II Regulates the Binding of Violaxanthin and Xanthophyll Cycle.Plant physiology · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major light harvesting complex II (LHCII) of green plants plays a key role in the absorption of sunlight, the regulation of photosynthesis, and in preventing photodamage by excess light. The latter two functions are thought to involve the lumenal loop and the N-terminal domain. Their structure and mobility in an aqueous environment are only partially known. Electron paramagnetic resonance (EPR) has been used to measure the structure of these hydrophilic protein domains in detergent-solubilized LHCII. A new technique is introduced to prepare LHCII trimers in which only one monomer is spin-labeled. These heterogeneous trimers allow to measure intra-molecular distances within one LHCII monomer in the context of a trimer by using double electron-electron resonance (DEER). These data together with data from electron spin echo envelope modulation (ESEEM) allowed to model the N-terminal protein section, which has not been resolved in current crystal structures, and the lumenal loop domain. The N-terminal domain covers only a restricted area above the superhelix in LHCII, which is consistent with the "Velcro" hypothesis to explain thylakoid grana stacking (Standfuss, J., van Terwisscha Scheltinga, A. C., Lamborghini, M., and Kühlbrandt, W. (2005) EMBO J. 24, 919-928). The conformation of the lumenal loop domain is surprisingly different between LHCII monomers and trimers but not between complexes with and without neoxanthin bound.
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