8wm6
The structure of PSI-CAC(L-14)of R.salina at 2.7 angstroms resolutionThe structure of PSI-CAC(L-14)of R.salina at 2.7 angstroms resolution
Structural highlights
FunctionA6MVZ7_RHDSA PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.[HAMAP-Rule:MF_00458] Publication Abstract from PubMedPhotosynthetic cryptophytes are eukaryotic algae that utilize membrane-embedded chlorophyll a/c binding proteins (CACs) and lumen-localized phycobiliproteins (PBPs) as their light-harvesting antennae. Cryptophytes go through logarithmic and stationary growth phases, and may adjust their light-harvesting capability according to their particular growth state. How cryptophytes change the type/arrangement of the photosynthetic antenna proteins to regulate their light-harvesting remains unknown. Here we solve four structures of cryptophyte photosystem I (PSI) bound with CACs that show the rearrangement of CACs at different growth phases. We identify a cryptophyte-unique protein, PsaQ, which harbors two chlorophyll molecules. PsaQ specifically binds to the lumenal region of PSI during logarithmic growth phase and may assist the association of PBPs with photosystems and energy transfer from PBPs to photosystems. Growth phase-dependent reorganization of cryptophyte photosystem I antennae.,Zhang S, Si L, Su X, Zhao X, An X, Li M Commun Biol. 2024 May 11;7(1):560. doi: 10.1038/s42003-024-06268-5. PMID:38734819[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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