Structure of CyanoP at 2.8 Å: Implications for the Evolution and Function of the PsbP Subunit of Photosystem II

被引：45

作者：

Michoux, Franck ^{[2
]}

Takasaka, Kenji ^{[2
]}

Boehm, Marko ^{[2
]}

Nixon, Peter J. ^{[2
]}

Murray, James W. ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, London SW7 2AZ, England

[2] Univ London Imperial Coll Sci Technol & Med, Div Biol, London SW7 2AZ, England

来源：

BIOCHEMISTRY | 2010年 / 49卷 / 35期

基金：

英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

KDA EXTRINSIC PROTEIN; SYNECHOCYSTIS SP PCC-6803; CRYSTAL-STRUCTURE; ARABIDOPSIS-THALIANA; SPINACIA-OLERACEA; MANGANESE BINDING; HIGHER-PLANTS; DONOR SIDE; RESOLUTION; COMPLEX;

D O I：

10.1021/bi1011145

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We present here the crystal structure of CyanoP (Tlr2075) from Thermosynechococcus elongatus at 2.8 angstrom. CyanoP is a substoichiometric component of the isolated cyanobacterial Photosystem II (PSII) complex, distantly related to the PsbP extrinsic subunit of the oxygen-evolving P S I I 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.

引用

页码：7411 / 7413

页数：3

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