Resonance assignment of PsbP: an extrinsic protein from photosystem II of Spinacia oleracea
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F15%3A43888967" target="_blank" >RIV/60076658:12310/15:43888967 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/15:00472743
Result on the web
<a href="http://link.springer.com/article/10.1007%2Fs12104-015-9606-2" target="_blank" >http://link.springer.com/article/10.1007%2Fs12104-015-9606-2</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s12104-015-9606-2" target="_blank" >10.1007/s12104-015-9606-2</a>
Alternative languages
Result language
angličtina
Original language name
Resonance assignment of PsbP: an extrinsic protein from photosystem II of Spinacia oleracea
Original language description
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, Ca2+ 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 H-1, N-15 and C-13 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 p
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biomolecular NMR Assignments
ISSN
1874-2718
e-ISSN
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Volume of the periodical
9
Issue of the periodical within the volume
2
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
6
Pages from-to
341-346
UT code for WoS article
000361440100027
EID of the result in the Scopus database
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