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Structure of CyanoP at 2.8 A: implications for the evolution and function of the PsbP subunit of photosystem II .

Authors :
Michoux F
Takasaka K
Boehm M
Nixon PJ
Murray JW
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.

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