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9HYU

Cryo-EM structure of the Chromera velia PSI supercomplex at 1.84 Angstrom resolution

This is a non-PDB format compatible entry.
Summary for 9HYU
Entry DOI10.2210/pdb9hyu/pdb
EMDB information52518
DescriptorSuperoxide dismutase [Fe], Photosystem I protein (PsaM), Photosystem I protein (PsaR), ... (36 entities in total)
Functional Keywordsphotosynthesis, photosystem i, psi-fcp complex, chrome velia, cryo-em.
Biological sourceChromera velia
More
Total number of polymer chains19
Total formula weight826448.78
Authors
Yuan, X.,Qian, P.,Sobotka, R.,Naschberger, A. (deposition date: 2025-01-10, release date: 2026-01-28, Last modification date: 2026-03-18)
Primary citationYuan, X.,Lukes, M.,Qian, P.,Charras, Q.,Smrcka, T.,Man, P.,Kovarova, L.,Konik, P.,Heilmann, E.,Al-Amoudi, A.,Sobotka, R.,Naschberger, A.
The cryo-EM structure of Photosystem I from Chromera velia with a bound superoxide dismutase heterodimer.
Nat Commun, 17:913-913, 2025
Cited by
PubMed Abstract: Photosystem I is a key component of the solar energy conversion machinery in oxygenic photosynthesis, and its core, where photochemistry occurs, is highly conserved. However, the coral-associated alga Chromera velia that is evolutionary linked to parasitic apicomplexans, exhibits Photosystem I with unusual features. These include the splitting of the central PsaA subunit and the binding of superoxide dismutases as regular subunits. The organization of such a unique Photosystem I was enigmatic. Here, we present the cryo-EM structure of Chromera velia Photosystem I at 1.84 Å resolution. Our work reveals a superoxide dismutase heterodimer bound to the stromal side of the core, stabilized by extensions of canonical subunits, a novel protein PsaV, and a reduced light-harvesting apparatus. We elucidate how the complex evolved to accommodate the superoxide dismutase, assemble the split PsaA, and integrate antenna proteins in a non-canonical orientation. Based on our data and prior physiological data, we propose that this specialized Photosystem I functions likely as an Mehler machine, redirecting electrons from Photosystem II back to water. This mechanism enables Chromera velia to manage redox imbalance and reduce photorespiration through localized oxygen consumption.
PubMed: 41423677
DOI: 10.1038/s41467-025-67637-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (1.84 Å)
Structure validation

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PDB entries from 2026-03-18

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