Literature summary for 2.7.13.3 extracted from

Otrusinova, O.; Demo, G.; Padrta, P.; Jasenakova, Z.; Pekarova, B.; Gelova, Z.; Szmitkowska, A.; Kaderavek, P.; Jansen, S.; Zachrdla, M.; Klumpler, T.; Marek, J.; Hritz, J.; Janda, L.; Iwai, H.; Wimmerova, M.; Hejatko, J.; Zidek, L.
Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana (2017), J. Biol. Chem., 292, 17525-17540 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of free, Mg2+-bound, and beryllofluoridated CKI1RD (a stable analogue of the labile phosphorylated form) are identical and similar to the active state of receiver domains of bacterial response regulator. Mg2+ binding and beryllofluoridation alter the conformational equilibrium of the beta3-alpha3 loop close to the phosphorylation site. Mutations that perturbe the conformational behavior of the beta3-alpha3 loop while keeping the active-site aspartate intact result in suppression of CKI1 function. The beta3-alpha3 loop may directly interact with the ATP-binding site of the CKI1 histidine kinase domain	Arabidopsis thaliana

Crystallization (Comment)

Organism

structures of free, Mg2+-bound, and beryllofluoridated CKI1RD (a stable analogue of the labile phosphorylated form) are identical and similar to the active state of receiver domains of bacterial response regulator. Mg2+ binding and beryllofluoridation alter the conformational equilibrium of the beta3-alpha3 loop close to the phosphorylation site. Mutations that perturbe the conformational behavior of the beta3-alpha3 loop while keeping the active-site aspartate intact result in suppression of CKI1 function. The beta3-alpha3 loop may directly interact with the ATP-binding site of the CKI1 histidine kinase domain

Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
D1050A	mutation changes conformation of the beta3-alpha3 loop in solution and shifts residue F1102 to the inactive orientation	Arabidopsis thaliana
D1050E	mutation changes conformation of the beta3-alpha3 loop in solution and shifts residue F1102 to the inactive orientation	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	O22267	-	-

Synonyms

Synonyms	Comment	Organism
CKI1	-	Arabidopsis thaliana
CYTOKININ-INDEPENDENT 1	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)