Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F15%3A43888968" target="_blank" >RIV/60076658:12310/15:43888968 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/15:00472747
Result on the web
<a href="http://onlinelibrary.wiley.com/doi/10.1002/prot.24853/abstract" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1002/prot.24853/abstract</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/prot.24853" target="_blank" >10.1002/prot.24853</a>
Alternative languages
Result language
angličtina
Original language name
Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants
Original language description
The extrinsic proteins of photosystem II of higher plants and green algae PsbO, PsbP, PsbQ, and PsbR are essential for stable oxygen production in the oxygen evolving center. In the available X-ray crystallographic structure of higher plant PsbQ residuesS14-Y33 are missing. Building on the backbone NMR assignment of PsbQ, which includes this missing link, we report the extended resonance assignment including side chain atoms. Based on nuclear Overhauser effect spectra a high resolution solution structure of PsbQ with a backbone RMSD of 0.81 angstrom was obtained from torsion angle dynamics. Within the N-terminal residues 1-45 the solution structure deviates significantly from the X-ray crystallographic one, while the four-helix bundle core found previously is confirmed. A short -helix is observed in the solution structure at the location where a -strand had been proposed in the earlier crystallographic study. NMR relaxation data and unrestrained molecular dynamics simulations corrobor
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
PROTEINS : Structure, Function, and Bioinformatics
ISSN
0887-3585
e-ISSN
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Volume of the periodical
83
Issue of the periodical within the volume
9
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
1677-1686
UT code for WoS article
000360242000013
EID of the result in the Scopus database
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