Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00472747

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

PROTEINS : Structure, Function, and Bioinformatics

ISSN

0887-3585

e-ISSN

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Svazek periodika

83

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

1677-1686

Kód UT WoS článku

000360242000013

EID výsledku v databázi Scopus

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