Advanced search
1 file | 2.15 MB Add to list

Crystal structure of Arabidopsis thaliana casein kinase 2 α1

Author
Organization
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 alpha 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.
Keywords
Biophysics, Genetics, Biochemistry, Structural Biology, Condensed Matter Physics, Casein Kinase, CK2, Structural Flexibility, ATP Binding, Arabidopsis Thaliana, Catalytic Subunit, Conformational Plasticity, CK2 Inhibitors, Zea-mays, Protein, Site, ATP, Discovery, CK2-alpha, Features

Downloads

  • Demulder et al. 2020 Acta Crystallogr. F-Struct. Biol. Commun. 76 182.pdf
    • full text (Published version)
    • |
    • open access
    • |
    • PDF
    • |
    • 2.15 MB

Citation

Please use this url to cite or link to this publication:

MLA
Demulder, Manon, et al. “Crystal Structure of Arabidopsis Thaliana Casein Kinase 2 Α1.” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, vol. 76, no. 4, 2020, pp. 182–91, doi:10.1107/s2053230x20004537.
APA
Demulder, M., De Veylder, L., & Loris, R. (2020). Crystal structure of Arabidopsis thaliana casein kinase 2 α1. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 76(4), 182–191. https://doi.org/10.1107/s2053230x20004537
Chicago author-date
Demulder, Manon, Lieven De Veylder, and Remy Loris. 2020. “Crystal Structure of Arabidopsis Thaliana Casein Kinase 2 Α1.” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 76 (4): 182–91. https://doi.org/10.1107/s2053230x20004537.
Chicago author-date (all authors)
Demulder, Manon, Lieven De Veylder, and Remy Loris. 2020. “Crystal Structure of Arabidopsis Thaliana Casein Kinase 2 Α1.” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 76 (4): 182–191. doi:10.1107/s2053230x20004537.
Vancouver
1.
Demulder M, De Veylder L, Loris R. Crystal structure of Arabidopsis thaliana casein kinase 2 α1. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS. 2020;76(4):182–91.
IEEE
[1]
M. Demulder, L. De Veylder, and R. Loris, “Crystal structure of Arabidopsis thaliana casein kinase 2 α1,” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, vol. 76, no. 4, pp. 182–191, 2020.
@article{8660086,
  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 alpha 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.}},
  author       = {{Demulder, Manon and De Veylder, Lieven and Loris, Remy}},
  issn         = {{2053-230X}},
  journal      = {{ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}},
  keywords     = {{Biophysics,Genetics,Biochemistry,Structural Biology,Condensed Matter Physics,Casein Kinase,CK2,Structural Flexibility,ATP Binding,Arabidopsis Thaliana,Catalytic Subunit,Conformational Plasticity,CK2 Inhibitors,Zea-mays,Protein,Site,ATP,Discovery,CK2-alpha,Features}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{182--191}},
  title        = {{Crystal structure of Arabidopsis thaliana casein kinase 2 α1}},
  url          = {{http://dx.doi.org/10.1107/s2053230x20004537}},
  volume       = {{76}},
  year         = {{2020}},
}

Altmetric
View in Altmetric
Web of Science
Times cited: