Crystal structure of CKI1 receiver domain from Arabidopsis

a 2009

Crystal structure of CKI1 receiver domain from Arabidopsis

KLUMPLER, Tomáš; Blanka PEKÁROVÁ; Jaromir MAREK; Lubomír JANDA; Jan HEJÁTKO et al.

Základní údaje

Originální název

Crystal structure of CKI1 receiver domain from Arabidopsis

Autoři

KLUMPLER, Tomáš; Blanka PEKÁROVÁ ; Jaromir MAREK ; Lubomír JANDA a Jan HEJÁTKO

Vydání

7th International Conference of Ph.D Students on Experimental Plant Biology "News - what the plants told us". Brno, 2009

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

Genetika a molekulární biologie

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/09:00039825

Organizační jednotka

Přírodovědecká fakulta

ISBN

978-80-7375-310-8

Klíčová slova anglicky

Arabidopsis cytokinin signaling CKI1 crystallography crystal structure

Změněno: 31. 3. 2010 10:36, Mgr. Tomáš Klumpler, Ph.D.

Anotace

V originále

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.

Návaznosti

LC06034, projekt VaV

Název: Regulace morfogeneze rostlinných buněk a orgánů

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Regulace morfogeneze rostlinných buněk a orgánů

MSM0021622415, záměr

Název: Molekulární podstata buněčných a tkáňových regulací

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Molekulární podstata buněčných a tkáňových regulací

Citovat

KLUMPLER, Tomáš; Blanka PEKÁROVÁ; Jaromir MAREK; Lubomír JANDA a Jan HEJÁTKO. Crystal structure of CKI1 receiver domain from Arabidopsis. In 7th International Conference of Ph.D Students on Experimental Plant Biology "News - what the plants told us". Brno. 2009. ISBN 978-80-7375-310-8.

@proceedings{878428,
   author = {Klumpler, Tomáš and Pekárová, Blanka and Marek, Jaromir and Janda, Lubomír and Hejátko, Jan},
   booktitle = {7th International Conference of Ph.D Students on Experimental Plant Biology "News - what the plants told us". Brno},
   keywords = {Arabidopsis cytokinin signaling CKI1 crystallography crystal structure},
   language = {eng},
   isbn = {978-80-7375-310-8},
   title = {Crystal structure of CKI1 receiver domain from Arabidopsis},
   year = {2009}
}

TY  - CONF
ID  - 878428
AU  - Klumpler, Tomáš - Pekárová, Blanka - Marek, Jaromir - Janda, Lubomír - Hejátko, Jan
PY  - 2009
TI  - Crystal structure of CKI1 receiver domain from Arabidopsis
SN  - 9788073753108
KW  - Arabidopsis cytokinin signaling CKI1 crystallography crystal structure
N2  - 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.
ER  -

KLUMPLER, Tomáš; Blanka PEKÁROVÁ; Jaromir MAREK; Lubomír JANDA a Jan HEJÁTKO. Crystal structure of CKI1 receiver domain from Arabidopsis. In \textit{7th International Conference of Ph.D Students on Experimental Plant Biology ''News - what the plants told us''. Brno}. 2009. ISBN~978-80-7375-310-8.

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