PDBsum entry 2bdw

Transferase

PDB id: 2bdw

Contents

Protein chains

309 a.a. *

Waters ×431

* Residue conservation analysis

PDB id:

2bdw

Name:

Transferase

Title:

Crystal structure of the auto-inhibited kinase domain of calcium/calmodulin activated kinase ii

Structure:

Hypothetical protein k11e8.1d. Chain: a, b. Fragment: auto-inhibited kinase domain fragment. Engineered: yes. Mutation: yes

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Gene: ca2+/calmodulin-dependent protein kinase. Unc-43 (k11e8.1d). Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

1.80Å R-factor: 0.216 R-free: 0.236

Authors:

O.S.Rosenberg,J.Kuriyan

Key ref:

O.S.Rosenberg et al. (2005). Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme. Cell, 123, 849-860. PubMed id: 16325579 DOI: 10.1016/j.cell.2005.10.029

Date:

20-Oct-05 Release date: 13-Dec-05

Protein chains

O62305  (KCC2D_CAEEL) -  Calcium/calmodulin-dependent protein kinase type II from Caenorhabditis elegans

Seq: 720 a.a.

Struc: 309 a.a.*

* PDB and UniProt seqs differ at 12 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.7.11.17 - calcium/calmodulin-dependent protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺
• Cofactor: Ca(2+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.cell.2005.10.029

Cell 123:849-860 (2005)

PubMed id: 16325579

Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme.

O.S.Rosenberg, S.Deindl, R.J.Sung, A.C.Nairn, J.Kuriyan.

ABSTRACT

Ca2+/calmodulin-dependent protein kinase-II (CaMKII) is unique among protein kinases for its dodecameric assembly and its complex response to Ca2+. The crystal structure of the autoinhibited kinase domain of CaMKII, determined at 1.8 A resolution, reveals an unexpected dimeric organization in which the calmodulin-responsive regulatory segments form a coiled-coil strut that blocks peptide and ATP binding to the otherwise intrinsically active kinase domains. A threonine residue in the regulatory segment, which when phosphorylated renders CaMKII calmodulin independent, is held apart from the catalytic sites by the organization of the dimer. This ensures a strict Ca2+ dependence for initial activation. The structure of the kinase dimer, when combined with small-angle X-ray scattering data for the holoenzyme, suggests that inactive CaMKII forms tightly packed autoinhibited assemblies that convert upon activation into clusters of loosely tethered and independent kinase domains.

Selected figure(s)

Figure 2.
Figure 2. Details of the Interaction between the Kinase Domain and the Regulatory Segment

Figure 3.
Figure 3. An Allosteric Mechanism Affecting the ATP Binding Site

The above figures are reprinted by permission from Cell Press: Cell (2005, 123, 849-860) copyright 2005.

Figures were selected by an automated process.