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Resonance assignment of PsbP: an extrinsic protein from photosystem II of Spinacia oleracea

A. Rathner, K. Chandra, P. Rathner, M. Horničáková, J. Schlagnitweit, J. Kohoutová, R. Ettrich, N. Müller,

. 2015 ; 9 (2) : 341-6. [pub] 20150423

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc16020858

PsbP (23 kDa) is an extrinsic eukaryotic protein of photosystem II found in the thylakoid membrane of higher plants and green algae. It has been proven to be indispensable for proper functioning of the oxygen evolving complex. By interaction with other extrinsic proteins (PsbQ, PsbO and PsbR), it modulates the concentration of two cofactors of the water splitting reaction, Ca(2+) and Cl(-). The crystallographic structure of PsbP from Spinacia oleracea lacks the N-terminal part as well as two inner regions which were modelled as loops. Those unresolved parts are believed to be functionally crucial for the binding of PsbP to the thylakoid membrane. In this NMR study we report (1)H, (15)N and (13)C resonance assignments of the backbone and side chain atoms of the PsbP protein. Based on these data, an estimate of the secondary structure has been made. The structural motifs found fit the resolved parts of the crystallographic structure very well. In addition, the complete assignment set provides preliminary insight into the dynamic regions.

Citace poskytuje Crossref.org

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$a PsbP (23 kDa) is an extrinsic eukaryotic protein of photosystem II found in the thylakoid membrane of higher plants and green algae. It has been proven to be indispensable for proper functioning of the oxygen evolving complex. By interaction with other extrinsic proteins (PsbQ, PsbO and PsbR), it modulates the concentration of two cofactors of the water splitting reaction, Ca(2+) and Cl(-). The crystallographic structure of PsbP from Spinacia oleracea lacks the N-terminal part as well as two inner regions which were modelled as loops. Those unresolved parts are believed to be functionally crucial for the binding of PsbP to the thylakoid membrane. In this NMR study we report (1)H, (15)N and (13)C resonance assignments of the backbone and side chain atoms of the PsbP protein. Based on these data, an estimate of the secondary structure has been made. The structural motifs found fit the resolved parts of the crystallographic structure very well. In addition, the complete assignment set provides preliminary insight into the dynamic regions.
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$a Rathner, Petr $u Institute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria. Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic.
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$a Horničáková, Michaela $u Institute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria. Lohmann Animal Health, Heinz-Lohmann-Straße 4, 27472, Cuxhaven, Germany.
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$a Schlagnitweit, Judith $u Institute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria. Centre de RMN à très Hauts Champs, Institut des Sciences Analytiques, Université de Lyon, 5 Rue de la Doua, 69100, Villeurbanne, France.
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$a Kohoutová, Jaroslava $u Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic. Centrum of Nanobiology and Structural Biology, Institute of Microbiology, Academy of Sciences of the Czech Republic, Nové Hrady, Czech Republic.
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$a Ettrich, Rüdiger $u Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic. Centrum of Nanobiology and Structural Biology, Institute of Microbiology, Academy of Sciences of the Czech Republic, Nové Hrady, Czech Republic.
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$a Müller, Norbert $u Institute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria. norbert.mueller@jku.at. Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic. norbert.mueller@jku.at.
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