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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00472743

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

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

Biomolecular NMR Assignments

ISSN

1874-2718

e-ISSN

—

Svazek periodika

9

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

341-346

Kód UT WoS článku

000361440100027

EID výsledku v databázi Scopus

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