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Structure of CyanoP at 2.8 A: implications for the evolution and function of the PsbP subunit of photosystem II .
- Source :
-
Biochemistry [Biochemistry] 2010 Sep 07; Vol. 49 (35), pp. 7411-3. - Publication Year :
- 2010
-
Abstract
- We present here the crystal structure of CyanoP (Tlr2075) from Thermosynechococcus elongatus at 2.8 A. CyanoP is a substoichiometric component of the isolated cyanobacterial Photosystem II (PSII) complex, distantly related to the PsbP extrinsic subunit of the oxygen-evolving PSII complex in higher plants and green algae. Despite the relatively low degree of sequence similarity, we have found that CyanoP adopts the same beta-sandwich fold as higher-plant PsbP and contains a well-conserved metal (zinc)-binding site that is also present in plant PsbP. Our results support the idea that CyanoP represents the basal structural fold of the PsbP superfamily.
- Subjects :
- Bacterial Proteins metabolism
Binding Sites
Crystallography, X-Ray
Evolution, Molecular
Models, Molecular
Oxygen chemistry
Oxygen metabolism
Photosystem II Protein Complex metabolism
Protein Conformation
Protein Folding
Protein Subunits chemistry
Protein Subunits metabolism
Zinc chemistry
Zinc metabolism
Bacterial Proteins chemistry
Cyanobacteria metabolism
Photosystem II Protein Complex chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 49
- Issue :
- 35
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 20698571
- Full Text :
- https://doi.org/10.1021/bi1011145