Crystal structure of CKI1 receiver domain from Arabidopsis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F09%3A00039825" target="_blank" >RIV/00216224:14310/09:00039825 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Crystal structure of CKI1 receiver domain from Arabidopsis

Popis výsledku v původním jazyce

Sensor histidine kinases (HKs) are members of the two-component (TC) signalling systems that mediate signal transduction in a broad spectrum of adaptive responses in bacteria. The sensor histidine kinase CKI1 was identified as an activator of a cytokinin-like response when overexpressed in hypocotyl explants of A. thaliana. However, in contrast to the genuine cytokinin receptors of A. thaliana, AHK2, AHK3 and AHK4, CKI1 was found to be constitutively active in bacteria and yeast or A. thaliana protoplasts. Thus, the specificity and the role of CKI1 in the TC signalling in A. thaliana remain unclear. The three-dimensional structure of A. thaliana CKI1RD was determined. The catalytic aspartate residue is located on the carboxyl terminus of the central beta3-strand, in a cavity formed by loops L1, L5 and L7 loops. All major conformational differences between receiver proteins are located in the loops, which supposedly form a docking interface for the ineracting partners.

Název v anglickém jazyce

Crystal structure of CKI1 receiver domain from Arabidopsis

Popis výsledku anglicky

Sensor histidine kinases (HKs) are members of the two-component (TC) signalling systems that mediate signal transduction in a broad spectrum of adaptive responses in bacteria. The sensor histidine kinase CKI1 was identified as an activator of a cytokinin-like response when overexpressed in hypocotyl explants of A. thaliana. However, in contrast to the genuine cytokinin receptors of A. thaliana, AHK2, AHK3 and AHK4, CKI1 was found to be constitutively active in bacteria and yeast or A. thaliana protoplasts. Thus, the specificity and the role of CKI1 in the TC signalling in A. thaliana remain unclear. The three-dimensional structure of A. thaliana CKI1RD was determined. The catalytic aspartate residue is located on the carboxyl terminus of the central beta3-strand, in a cavity formed by loops L1, L5 and L7 loops. All major conformational differences between receiver proteins are located in the loops, which supposedly form a docking interface for the ineracting partners.

Druh

O - Ostatní výsledky

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

<a href="/cs/project/LC06034" target="_blank" >LC06034: Regulace morfogeneze rostlinných buněk a orgánů</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

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