2021
DOI: 10.1101/2021.01.15.426676
|View full text |Cite
Preprint
|
Sign up to set email alerts
|

High-resolution model of Arabidopsis Photosystem II reveals the consequences of digitonin-extraction

Abstract: In higher plants, the photosynthetic process is performed and regulated by Photosystem II (PSII). Arabidopsis thaliana was the first higher plant with a fully sequenced genome, conferring it the status of a model organism; nonetheless, a high-resolution structure of its Photosystem II is missing. We present the first Cryo-EM high-resolution structure of Arabidopsis PSII supercomplex with average resolution of 2.79 Å, an important model for future PSII studies. The digitonin extracted PSII complexes demonstrate… Show more

Help me understand this report
View published versions

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2022
2022
2022
2022

Publication Types

Select...
2

Relationship

0
2

Authors

Journals

citations
Cited by 2 publications
(1 citation statement)
references
References 61 publications
0
1
0
Order By: Relevance
“…The homology models cannot capture the positions of most of the N-terminal residues that comprise the FRL-specific extension of FRL-PsbH or that of its ancestral sequence, and even the residues that can be modeled in the N-terminal regions are likely positioned with low confidence, but the FRLspecific N-terminal extensions could alter the region of the SQD and/or the other interactions at the dimerization interface. Furthermore, it was surprising that the apo-FRL-PSII structure lacked FRL-PsbH, as PsbH is found in all other cryo-EM structures of PSII, even assembly intermediate-like-, apo-, and monomeric-PSII complexes [54][55][56][57]. These observations suggest that FRL-PsbH binds less tightly to the FRL-PSII complex relative to VL-PsbH, which could have implications for details of assembly and repair.…”
Section: Conserved Features Of Frl-psbhmentioning
confidence: 99%
“…The homology models cannot capture the positions of most of the N-terminal residues that comprise the FRL-specific extension of FRL-PsbH or that of its ancestral sequence, and even the residues that can be modeled in the N-terminal regions are likely positioned with low confidence, but the FRLspecific N-terminal extensions could alter the region of the SQD and/or the other interactions at the dimerization interface. Furthermore, it was surprising that the apo-FRL-PSII structure lacked FRL-PsbH, as PsbH is found in all other cryo-EM structures of PSII, even assembly intermediate-like-, apo-, and monomeric-PSII complexes [54][55][56][57]. These observations suggest that FRL-PsbH binds less tightly to the FRL-PSII complex relative to VL-PsbH, which could have implications for details of assembly and repair.…”
Section: Conserved Features Of Frl-psbhmentioning
confidence: 99%