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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,
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Photosystem II Protein Complex chemistry MeSH
- Crystallography, X-Ray MeSH
- Molecular Sequence Data MeSH
- Proton Magnetic Resonance Spectroscopy * MeSH
- Plant Proteins chemistry MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Spinacia oleracea chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by 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 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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