Sequence Analysis of the D1 and D2 Reaction Center Proteins of Photosystem II

Bengt Svensson; Imre Vass; Stenbjörn Styring

doi:10.1515/znc-1991-9-1008

Sequence Analysis of the D1 and D2 Reaction Center Proteins of Photosystem II

Bengt Svensson, Imre Vass, Stenbjörn Styring

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-review

152 Scopus citations

Abstract

A compilation of 38 sequences for the D1 and 15 sequences for the D2 reaction center proteins of photosystem II is presented. The sequences have been compared and a similarity index that takes into account the degree of conservation and the quality of the changes in each position has been calculated. The similarity index is used to identify and describe functionally important domains in the D1/D2 heterodimer. Comparative hydropathy plot are presented for the aminoacid sidechains that constitute the binding domain of the tyrosine radicals, Tyr_z and Tyr_D in photosystem II. The structure around Tyr_z is more hydrophilic than the structure around Tyr_D. The hydrophilic residues are clustered in the part of the binding pocket for Tyr_z that is turned towards the lumenal side of the thylakoid membrane. Most prominent is the presence of two conserved carboxylic aminoacids, Dl-Asp 170 and Dl-Glu 189. Their respective carboxyl-groups come close in space and are proposed to constitute a metal binding site together with Dl-Gln 165. The distance between the proposed metal binding site and the center of the ring of Tyr_z is approximately 7 A. The cavity that constitutes the binding site for Tyr_D is composed of residues from the D2 protein. Its character is more hydrophobic than the Tyr_z site and the environment around Tyr_D lacks the cluster of putative metal binding side-chains.

Original language	English (US)
Pages (from-to)	765-776
Number of pages	12
Journal	Zeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume	46
Issue number	9-10
DOIs	https://doi.org/10.1515/znc-1991-9-1008
State	Published - Oct 1 1991

Bibliographical note

Funding Information:
M. Degli Esposti and M. Crimi are gratefully acknowledged for providing us with the program QMAGINT for the hydropathy plots. Mr. Bo Furugren is thanked for help with Fig. 2A. I.V. was supported by a visiting scientist fellowship from the Foundation Wenner-Grenska Samfun-det, Stockholm. The work was supported from the Swedish Natural Science Research Council, the Erna and Victor Hasselblad Foundation and the Knut and Alice Wallenbergs Foundation and the Carl Trygger Foundation.

Keywords

D1 Protein
D2 Protein
Manganese
Photosystem II
Reaction Center
Tyrosine

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title = "Sequence Analysis of the D1 and D2 Reaction Center Proteins of Photosystem II",

abstract = "A compilation of 38 sequences for the D1 and 15 sequences for the D2 reaction center proteins of photosystem II is presented. The sequences have been compared and a similarity index that takes into account the degree of conservation and the quality of the changes in each position has been calculated. The similarity index is used to identify and describe functionally important domains in the D1/D2 heterodimer. Comparative hydropathy plot are presented for the aminoacid sidechains that constitute the binding domain of the tyrosine radicals, Tyrz and TyrD in photosystem II. The structure around Tyrz is more hydrophilic than the structure around TyrD. The hydrophilic residues are clustered in the part of the binding pocket for Tyrz that is turned towards the lumenal side of the thylakoid membrane. Most prominent is the presence of two conserved carboxylic aminoacids, Dl-Asp 170 and Dl-Glu 189. Their respective carboxyl-groups come close in space and are proposed to constitute a metal binding site together with Dl-Gln 165. The distance between the proposed metal binding site and the center of the ring of Tyrz is approximately 7 A. The cavity that constitutes the binding site for TyrD is composed of residues from the D2 protein. Its character is more hydrophobic than the Tyrz site and the environment around TyrD lacks the cluster of putative metal binding side-chains.",

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author = "Bengt Svensson and Imre Vass and Stenbj{\"o}rn Styring",

note = "Funding Information: M. Degli Esposti and M. Crimi are gratefully acknowledged for providing us with the program QMAGINT for the hydropathy plots. Mr. Bo Furugren is thanked for help with Fig. 2A. I.V. was supported by a visiting scientist fellowship from the Foundation Wenner-Grenska Samfun-det, Stockholm. The work was supported from the Swedish Natural Science Research Council, the Erna and Victor Hasselblad Foundation and the Knut and Alice Wallenbergs Foundation and the Carl Trygger Foundation.",

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N2 - A compilation of 38 sequences for the D1 and 15 sequences for the D2 reaction center proteins of photosystem II is presented. The sequences have been compared and a similarity index that takes into account the degree of conservation and the quality of the changes in each position has been calculated. The similarity index is used to identify and describe functionally important domains in the D1/D2 heterodimer. Comparative hydropathy plot are presented for the aminoacid sidechains that constitute the binding domain of the tyrosine radicals, Tyrz and TyrD in photosystem II. The structure around Tyrz is more hydrophilic than the structure around TyrD. The hydrophilic residues are clustered in the part of the binding pocket for Tyrz that is turned towards the lumenal side of the thylakoid membrane. Most prominent is the presence of two conserved carboxylic aminoacids, Dl-Asp 170 and Dl-Glu 189. Their respective carboxyl-groups come close in space and are proposed to constitute a metal binding site together with Dl-Gln 165. The distance between the proposed metal binding site and the center of the ring of Tyrz is approximately 7 A. The cavity that constitutes the binding site for TyrD is composed of residues from the D2 protein. Its character is more hydrophobic than the Tyrz site and the environment around TyrD lacks the cluster of putative metal binding side-chains.

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Sequence Analysis of the D1 and D2 Reaction Center Proteins of Photosystem II

Abstract

Bibliographical note

Keywords

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