Crystal structure of the Psb28 accessory factor of Thermosynechococcus elongatus photosystem II at 2.3 angstrom

Kód výsledku v IS VaVaI

RIV/60076658:12310/13:43885355 - isvavai.cz

Nalezeny alternativní kódy

RIV/61388971:_____/13:00424558

Výsledek na webu

http://download.springer.com/static/pdf/102/art%253A10.1007%252Fs11120-013-9939-6.pdf?auth66=1389878061_c20a4cc6884ad87daa24ae6eeb47b654&ext=.pdf

DOI - Digital Object Identifier

10.1007/s11120-013-9939-6

Jazyk výsledku

angličtina

Název v původním jazyce

Crystal structure of the Psb28 accessory factor of Thermosynechococcus elongatus photosystem II at 2.3 angstrom

Popis výsledku v původním jazyce

Members of the Psb28 family of proteins are accessory factors implicated in the assembly and repair of the photosystem II complex. We present here the crystal structure of the Psb28 protein (Tlr0493) found in the thermophilic cyanobacterium Thermosynechococcus elongatus at a resolution of 2.3 a"{{. Overall the crystal structure of the Psb28 monomer is similar to the solution structures of C-terminally His-tagged Psb28-1 from Synechocystis sp. PCC 6803 obtained previously by nuclear magnetic resonance spectroscopy. One new aspect is that Escherichia coli-expressed T. elongatus Psb28 is able to form dimers in solution and packs as a dimer of dimers in the crystal. Analysis of wild type and mutant strains of Synechocystis 6803 by blue native-polyacrylamide gel electrophoresis suggests that Psb28-1, the closest homologue to T. elongatus Psb28 in this organism, also exists as an oligomer in vivo, most likely a dimer. In line with the prediction based on the crystal structure of T. elongatus

Název v anglickém jazyce

Crystal structure of the Psb28 accessory factor of Thermosynechococcus elongatus photosystem II at 2.3 angstrom

Popis výsledku anglicky

Members of the Psb28 family of proteins are accessory factors implicated in the assembly and repair of the photosystem II complex. We present here the crystal structure of the Psb28 protein (Tlr0493) found in the thermophilic cyanobacterium Thermosynechococcus elongatus at a resolution of 2.3 a"{{. Overall the crystal structure of the Psb28 monomer is similar to the solution structures of C-terminally His-tagged Psb28-1 from Synechocystis sp. PCC 6803 obtained previously by nuclear magnetic resonance spectroscopy. One new aspect is that Escherichia coli-expressed T. elongatus Psb28 is able to form dimers in solution and packs as a dimer of dimers in the crystal. Analysis of wild type and mutant strains of Synechocystis 6803 by blue native-polyacrylamide gel electrophoresis suggests that Psb28-1, the closest homologue to T. elongatus Psb28 in this organism, also exists as an oligomer in vivo, most likely a dimer. In line with the prediction based on the crystal structure of T. elongatus

Druh

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

CEP obor

ED - Fyziologie

OECD FORD obor

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Projekt

ED2.1.00/03.0110: Centrum řasových biotechnologií Třeboň (Algatech)

Návaznosti

V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Rok uplatnění

2013

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

—

Svazek periodika

117

Číslo periodika v rámci svazku

1-3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

375-383

Kód UT WoS článku

000326604900026

EID výsledku v databázi Scopus

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