Structural characterization of photosystem II complex from red alga Porphyridium cruentum retaining extrinsic subunits of the oxygen-evolving complex
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15233792
DOI
10.1111/j.1432-1033.2004.04226.x
PII: EJB4226
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins chemistry genetics metabolism MeSH
- Algal Proteins chemistry genetics metabolism ultrastructure MeSH
- Photosystem II Protein Complex chemistry genetics metabolism ultrastructure MeSH
- Protein Structure, Quaternary * MeSH
- Oxygen metabolism MeSH
- Macromolecular Substances MeSH
- Models, Molecular MeSH
- Protein Subunits chemistry genetics metabolism MeSH
- Porphyridium chemistry cytology metabolism MeSH
- Thylakoids chemistry ultrastructure MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Algal Proteins MeSH
- Photosystem II Protein Complex MeSH
- Oxygen MeSH
- Macromolecular Substances MeSH
- Protein Subunits MeSH
The structure of photosystem II (PSII) complex isolated from thylakoid membranes of the red alga Porphyridium cruentum was investigated using electron microscopy followed by single particle image analysis. The dimeric complexes observed contain all major PSII subunits (CP47, CP43, D1 and D2 proteins) as well as the extrinsic proteins (33 kDa, 12 kDa and the cytochrome c(550)) of the oxygen-evolving complex (OEC) of PSII, encoded by the psbO, psbU and psbV genes, respectively. The single particle analysis of the top-view projections revealed the PSII complex to have maximal dimensions of 22 x 15 nm. The analysis of the side-view projections shows a maximal thickness of the PSII complex of about 9 nm including the densities on the lumenal surface that has been attributed to the proteins of the OEC complex. These results clearly demonstrate that the red algal PSII complex is structurally very similar to that of cyanobacteria and to the PSII core complex of higher plants. In addition, the arrangement of the OEC proteins on the lumenal surface of the PSII complex is consistent to that obtained by X-ray crystallography of cyanobacterial PSII.
References provided by Crossref.org
Phycobilisome Mobility and Its Role in the Regulation of Light Harvesting in Red Algae
Structure of PSI, PSII and antennae complexes from yellow-green alga Xanthonema debile
