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7BW2

Crystal Structure of Cyanobacterial PSI Monomer from T.elongatus at 6.5 A Resolution

Summary for 7BW2
Entry DOI10.2210/pdb7bw2/pdb
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (12 entities in total)
Functional Keywordsmonomer, complex, photosystem, photosynthesis, membrane protein
Biological sourceThermosynechococcus elongatus BP-1
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Total number of polymer chains12
Total formula weight258239.03
Authors
Kurisu, G.,Coruh, O.,Tanaka, H.,Eithar, E.M.,Mian, Y. (deposition date: 2020-04-13, release date: 2021-03-17, Last modification date: 2024-10-30)
Primary citationCoruh, O.,Frank, A.,Tanaka, H.,Kawamoto, A.,El-Mohsnawy, E.,Kato, T.,Namba, K.,Gerle, C.,Nowaczyk, M.M.,Kurisu, G.
Cryo-EM structure of a functional monomeric Photosystem I from Thermosynechococcus elongatus reveals red chlorophyll cluster.
Commun Biol, 4:304-304, 2021
Cited by
PubMed Abstract: A high-resolution structure of trimeric cyanobacterial Photosystem I (PSI) from Thermosynechococcus elongatus was reported as the first atomic model of PSI almost 20 years ago. However, the monomeric PSI structure has not yet been reported despite long-standing interest in its structure and extensive spectroscopic characterization of the loss of red chlorophylls upon monomerization. Here, we describe the structure of monomeric PSI from Thermosynechococcus elongatus BP-1. Comparison with the trimer structure gave detailed insights into monomerization-induced changes in both the central trimerization domain and the peripheral regions of the complex. Monomerization-induced loss of red chlorophylls is assigned to a cluster of chlorophylls adjacent to PsaX. Based on our findings, we propose a role of PsaX in the stabilization of red chlorophylls and that lipids of the surrounding membrane present a major source of thermal energy for uphill excitation energy transfer from red chlorophylls to P700.
PubMed: 33686186
DOI: 10.1038/s42003-021-01808-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (6.5 Å)
Structure validation

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