Evidence map›Paper›PMID 25903141›Full record

ArticleBiomolecular NMR assignments2015

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

Adriana Rathner, Kousik Chandra, Petr Rathner, Michaela Horničáková, Judith Schlagnitweit, Jaroslava Kohoutová, Rüdiger Ettrich, Norbert Müller

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In one paragraph

Article in Biomolecular NMR assignments, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Adriana RathnerInstitute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria.
Kousik ChandraInstitute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria.
Petr RathnerInstitute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria.
Michaela HorničákováInstitute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria.
Judith SchlagnitweitInstitute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria.
Jaroslava KohoutováFaculty of Science, University of South Bohemia, České Budějovice, Czech Republic.
Rüdiger EttrichFaculty of Science, University of South Bohemia, České Budějovice, Czech Republic.
Norbert MüllerInstitute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria. norbert.mueller@jku.at.

Funding

Austrian Science Fund FWF W 1250
6 · The paper itself

Abstract

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.

Indexed as

Proton Magnetic Resonance SpectroscopyAmino Acid SequenceCrystallography, X-RayMolecular Sequence DataPhotosystem II Protein ComplexPlant ProteinsProtein Structure, SecondarySpinacia oleraceaPhotosystem II Protein ComplexPlant ProteinsDynamic regionsIntrinsic disorderOxygen evolving complexPhotosystem IIPsbP

Identifiers

PMID25903141
PMCPMC4568021

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