The cryo-EM structure of Photosystem I from Chromera velia with a bound superoxide dismutase heterodimer
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F25%3A43910778" target="_blank" >RIV/60076658:12310/25:43910778 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/25:10510835
Result on the web
<a href="https://www.nature.com/articles/s41467-025-67637-0" target="_blank" >https://www.nature.com/articles/s41467-025-67637-0</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-025-67637-0" target="_blank" >10.1038/s41467-025-67637-0</a>
Alternative languages
Result language
angličtina
Original language name
The cryo-EM structure of Photosystem I from Chromera velia with a bound superoxide dismutase heterodimer
Original language description
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 & Aring; 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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
2041-1723
Volume of the periodical
17
Issue of the periodical within the volume
1
Country of publishing house
DE - GERMANY
Number of pages
16
Pages from-to
nestránkováno
UT code for WoS article
001668141300002
EID of the result in the Scopus database
2-s2.0-105028521458