Structural highlights
Function
Q8DH84_THEVB
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of CyanoP at 2.8 A: Implications for the Evolution and Function of the PsbP Subunit of Photosystem II .,Michoux F, Takasaka K, Boehm M, Nixon PJ, Murray JW Biochemistry. 2010 Aug 17. PMID:20698571[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Michoux F, Takasaka K, Boehm M, Nixon PJ, Murray JW. Structure of CyanoP at 2.8 A: Implications for the Evolution and Function of the PsbP Subunit of Photosystem II . Biochemistry. 2010 Aug 17. PMID:20698571 doi:10.1021/bi1011145