Published
Plant structural biology: A knowledge gap with a window of opportunity
Biología estructural vegetal: Una brecha de conocimiento con unaventana de oportunidad
DOI:
https://doi.org/10.15446/abc.v31n3.129828Keywords:
artificial intelligence, cryo-EM, cryo-ET, photosystem II, plant structural biology (en)biología estructural vegetal, crio-EM, crio-ET, fotosistema II, inteligencia artificial (es)
Downloads
Plant proteins remain underrepresented in structural databases, reflecting historical research priorities and technical limitations rather than lower biological complexity. Recent advances in cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), in-cell solid-state NMR, and artificial intelligence (AI)-based modelling are narrowing this gap and enabling structural analysis of previously inaccessible plant molecular assemblies. In this note, we highlight advances in five systems: photoreceptors, photosystem II, the TOC–TIC chloroplast protein-import complex, the plant 80S ribosome, and plastid ESCRT-III-type machinery. Together, these examples illustrate a methodological transition in plant structural biology. We argue that the major challenge is shifting from obtaining structures to understanding their mechanisms, dynamics, and integration within native cellular and physiological contexts. AI-based modelling offers substantial opportunities, but experimental validation remains essential.
Las proteínas vegetales siguen estando infrarrepresentadas en las bases de datos estructurales, lo que refleja prioridades históricas de investigación y limitaciones técnicas, más que una menor complejidad biológica. Los recientes avances en criomicroscopía electrónica (crio-EM), criotomografía electrónica (crio-ET), RMN de estado sólido in vivo y modelamiento basado en inteligencia artificial (IA) están reduciendo esta brecha y permitiendo el análisis estructural de ensamblajes moleculares vegetales previamente inaccesibles. En esta nota, destacamos los avances en cinco sistemas: fotorreceptores, fotosistema II, el complejo de importación de proteínas TOC-TIC del cloroplasto, el ribosoma 80S vegetal y la maquinaria tipo ESCRT-III del plastidio. En conjunto, estos ejemplos ilustran una transición metodológica en la biología estructural vegetal. Sostenemos que el principal desafío reside en pasar de la obtención de estructuras a la comprensión de sus mecanismos, dinámica e integración en contextos celulares y fisiológicos nativos. El modelamiento basado en IA ofrece oportunidades sustanciales, pero la validación experimental sigue siendo esencial.
References
Bai, X. C., McMullan, G. and Scheres, S. H. W. (2015). How cryo-EM is revolutionizing structural biology. Trends in Biochemical Sciences, 40(1), 49–57. https://doi.org/10.1016/j.tibs.2014.10.005
Böhm, J. M. and Maurino, V. G. (2026). Plant structural biology: Emerging technologies and future biological insights. The Plant Journal. 125(5). https://doi.org/10.1111/tpj.70786
Jin, Z., Wan, L., Zhang, Y., Li, X., Cao, Y., Liu, H., Fan, S., Cao, D., Wang, Z., Li, X., Pan, J., Dong, M.-Q., Wu, J. and Yan, Z. (2022). Structure of a TOC-TIC supercomplex spanning two chloroplast envelope membranes. Cell, 185(25), 4788–4800.e13. https://doi.org/10.1016/j.cell.2022.10.030
Kikuchi, S., Bédard, J., Hirano, M., Hirabayashi, Y., Oishi, M., Imai, M., Takase, M., Ide, T. and Nakai, M. (2013). Uncovering the protein translocon at the chloroplast inner envelope membrane. Science, 339(6119), 571–574. https://doi.org/10.1126/science.1229262
Kühlbrandt, W. (2014). Microscopy: Cryo-EM enters a new era. eLife, 3, e03678. https://doi.org/10.7554/eLife.03678
Kutzner, M., Junglas, B., Sharma, M., Sachse, C. and Schneider, D. (2026). Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins. The Plant Journal, 126(1), e70843. https://doi.org/10.1111/tpj.70843
Liang, K., Jin, Z., Zhan, X., Li, Y., Xu, Q., Xie, Y., Yang, Y., Wang, S., Wu, J. and Yan, Z. (2024). Structural insights into the chloroplast protein import in land plants. Cell, 187(20), 5651–5664.e18. https://doi.org/10.1016/j.cell.2024.08.003
Liu, H. and Lee, W. (2019). The XFEL protein crystallography: Developments and perspectives. International Journal of Molecular Sciences, 20(14), 3421. https://doi.org/10.3390/ijms20143421
Liu, H., Li, A., Rochaix, J. D. and Liu, Z. (2023). Architecture of chloroplast TOC–TIC translocon supercomplex. Nature, 615, 349–357. https://doi.org/10.1038/s41586-023-05744-y
Ma, L., Wang, L., Tian, D. and Yin, P. (2026). Advances in mechanistic understanding of light signal transduction derived from plant structural biology. The Plant Journal, 125(6), e70817. https://doi.org/10.1111/tpj.70817
Martin-Garcia, J. M., Conrad, C. E., Coe, J., Roy-Chowdhury, S. and Fromme, P. (2016). Serial femtosecond crystallography: A revolution in structural biology. Archives of Biochemistry and Biophysics, 602, 32–47. https://doi.org/10.1016/j.abb.2016.03.036
Murray, J. W. (2026). Recent advances in the structural biology of photosystem II. The Plant Journal, 126(4), e70925. https://doi.org/10.1111/tpj.70925
Nogales, E. and Mahamid, J. (2024). Bridging structural and cell biology with cryo-electron microscopy. Nature, 628(8006), 47–56. https://doi.org/10.1038/s41586-024-07198-2
Smirnova, J., Loerke, J., Kleinau, G., Schmidt, A., Bürger, J., Meyer, E. H., Mielke, T., Scheerer, P., Bock, R., Spahn, C. M. T. and Zoschke, R. (2023). Structure of the actively translating plant 80S ribosome at 2.2 Å resolution. Nature Plants, 9, 987–1000. https://doi.org/10.1038/s41477-023-01407-y
Varadi, M., Bertoni, D., Magana, P., Paramval, U., Pidruchna, I., Radhakrishnan, M., Tsenkov, M., Nair, S., Mirdita, M., Yeo, J., Kovalevskiy, O., Tunyasuvunakool, K., Laydon, A., Žídek, A., Tomlinson, H., Hariharan, D., Abrahamson, J., Green, T., Jumper, J., Birney, E., Steinegger, M., Hassabis, D. and Velankar, S. (2024). AlphaFold Protein Structure Database in 2024: Providing structure coverage for over 214 million protein sequences. Nucleic Acids Research, 52(D1), D368–D375. https://doi.org/10.1093/nar/gkad1011
Xie, H., Zhao, Y., Zhao, W., Chen, Y., Liu, M. and Yang, J. (2023). Solid-state NMR structure determination of a membrane protein in E. coli cellular inner membrane. Science Advances, 9(44), eadh4168. https://doi.org/10.1126/sciadv.adh4168
Xing, S., Pan, J. and Yang, W. (2025). Chloroplast protein translocation complexes and their regulation. Journal of Integrative Plant Biology. 67(4) https://doi.org/10.1111/jipb.13875
Dimensions
PlumX
Article abstract page views
Downloads
How to Cite
License
This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
The acceptance of manuscripts by the Journal implies its electronic edition of open Access under Creative Commons Attribution License 4.0, and the inclusion and diffusion of the complete text through the institutional repository of the Universidad Nacional de Colombia and in all the specialized data bases that the editor considers adequate for its indexation to increase Journal visibility.
Acta Biológica Colombiana allows authors to archive, download and distribute the final published version, as well as pre-print and post-print versions including a header with the bibliographic reference of published article. The journal encourages the authors to distribute the final versión through Internet, for example in their personal or institutional web pages, and scientific social networks.
