4.4 Article

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

Journal

BIOCHEMISTRY
Volume 49, Issue 35, Pages 7411-7413

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/bi1011145

Keywords

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Funding

  1. BBSRC [BB/F023308/1, BB/E006388/1]
  2. EPSRC [EP/F00270X/1]
  3. BBSRC [BB/F020554/1, BB/F023308/1, BB/E006388/1] Funding Source: UKRI
  4. EPSRC [EP/F00270X/1] Funding Source: UKRI
  5. Biotechnology and Biological Sciences Research Council [BB/F020554/1, BB/F023308/1, BB/E006388/1] Funding Source: researchfish
  6. Engineering and Physical Sciences Research Council [EP/F00270X/1] Funding Source: researchfish

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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.

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