Crystal structure of Arabidopsis thaliana casein kinase 2 α1.
Acta Crystallogr F Struct Biol Commun
; 76(Pt 4): 182-191, 2020 Apr 01.
Article
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| MEDLINE
| ID: mdl-32254052
ABSTRACT
Casein kinase 2 (CK2) is a ubiquitous pleiotropic enzyme that is highly conserved across eukaryotic kingdoms. CK2 is singular amongst kinases as it is highly rigid and constitutively active. Arabidopsis thaliana is widely used as a model system in molecular plant research; the biological functions of A. thaliana CK2 are well studied in vivo and many of its substrates have been identified. Here, crystal structures of the α subunit of A. thaliana CK2 in three crystal forms and of its complex with the nonhydrolyzable ATP analog AMppNHp are presented. While the C-lobe of the enzyme is highly rigid, structural plasticity is observed for the N-lobe. Small but significant displacements within the active cleft are necessary in order to avoid steric clashes with the AMppNHp molecule. Binding of AMppNHp is influenced by a rigid-body motion of the N-lobe that was not previously recognized in maize CK2.
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MEDLINE
Assunto principal:
Arabidopsis
/
Proteínas de Arabidopsis
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Caseína Quinase II
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article