Crystal structure of the Psb27 assembly factor at 1.6: implications for binding to Photosystem II

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00388577" target="_blank" >RIV/61388971:_____/12:00388577 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s11120-011-9712-7" target="_blank" >http://dx.doi.org/10.1007/s11120-011-9712-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11120-011-9712-7" target="_blank" >10.1007/s11120-011-9712-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Crystal structure of the Psb27 assembly factor at 1.6: implications for binding to Photosystem II

Popis výsledku v původním jazyce

The biogenesis and oxygen-evolving activity of cyanobacterial Photosystem II (PSII) is dependent on a number of accessory proteins not found in the crystallised dimeric complex. These include Psb27, a small lipoprotein attached to the lumenal side of PSII, which has been assigned a role in regulating the assembly of the Mn(4)Ca cluster catalysing water oxidation. To gain a better understanding of Psb27, we have determined in this study the crystal structure of the soluble domain of Psb27 from Thermosynechococcus elongatus to a resolution of 1.6 . The structure is a four-helix bundle, similar to the recently published solution structures of Psb27 from Synechocystis PCC 6803 obtained by nuclear magnetic resonance (NMR) spectroscopy. Importantly, the crystal structure presented here helps us resolve the differences between the NMR-derived structural models. Potential binding sites for Psb27 within PSII are discussed in light of recent biochemical data in the literature

Název v anglickém jazyce

Crystal structure of the Psb27 assembly factor at 1.6: implications for binding to Photosystem II

Popis výsledku anglicky

The biogenesis and oxygen-evolving activity of cyanobacterial Photosystem II (PSII) is dependent on a number of accessory proteins not found in the crystallised dimeric complex. These include Psb27, a small lipoprotein attached to the lumenal side of PSII, which has been assigned a role in regulating the assembly of the Mn(4)Ca cluster catalysing water oxidation. To gain a better understanding of Psb27, we have determined in this study the crystal structure of the soluble domain of Psb27 from Thermosynechococcus elongatus to a resolution of 1.6 . The structure is a four-helix bundle, similar to the recently published solution structures of Psb27 from Synechocystis PCC 6803 obtained by nuclear magnetic resonance (NMR) spectroscopy. Importantly, the crystal structure presented here helps us resolve the differences between the NMR-derived structural models. Potential binding sites for Psb27 within PSII are discussed in light of recent biochemical data in the literature

Druh

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

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Photosynthesis Research

ISSN

0166-8595

e-ISSN

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Svazek periodika

110

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

169-175

Kód UT WoS článku

000299507400002

EID výsledku v databázi Scopus

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