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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F09%3A00039825%21RIV10-MSM-14310___
rdf:type
n5:Vysledek skos:Concept
dcterms:description
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. 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.
dcterms:title
Crystal structure of CKI1 receiver domain from Arabidopsis Crystal structure of CKI1 receiver domain from Arabidopsis
skos:prefLabel
Crystal structure of CKI1 receiver domain from Arabidopsis Crystal structure of CKI1 receiver domain from Arabidopsis
skos:notation
RIV/00216224:14310/09:00039825!RIV10-MSM-14310___
n3:aktivita
n6:Z n6:P
n3:aktivity
P(LC06034), Z(MSM0021622415)
n3:dodaniDat
n9:2010
n3:domaciTvurceVysledku
n4:1645102 n4:6980058 n4:8675058 n4:6662072 n4:5410142
n3:druhVysledku
n12:O
n3:duvernostUdaju
n10:S
n3:entitaPredkladatele
n8:predkladatel
n3:idSjednocenehoVysledku
308606
n3:idVysledku
RIV/00216224:14310/09:00039825
n3:jazykVysledku
n18:eng
n3:klicovaSlova
Arabidopsis cytokinin signaling CKI1 crystallography crystal structure
n3:klicoveSlovo
n17:Arabidopsis%20cytokinin%20signaling%20CKI1%20crystallography%20crystal%20structure
n3:kontrolniKodProRIV
[21B75DC97170]
n3:obor
n15:EB
n3:pocetDomacichTvurcuVysledku
5
n3:pocetTvurcuVysledku
5
n3:projekt
n16:LC06034
n3:rokUplatneniVysledku
n9:2009
n3:tvurceVysledku
Janda, Lubomír Marek, Jaromír Klumpler, Tomáš Hejátko, Jan Pekárová, Blanka
n3:zamer
n14:MSM0021622415
n11:organizacniJednotka
14310