PDBsum entry: 1iaj

Transferase

PDB id: 1iaj

Contents

Protein chains

253 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

1iaj

Name:

Transferase

Title:

Crystal structure of the atypical protein kinase domain of a trp ca-channel, chak (apo)

Structure:

Transient receptor potential-related protein. Chain: a, b. Fragment: protein kinase domain, residues 1549-1828. Synonym: trp-related. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: chak. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.80Å R-factor: 0.229 R-free: 0.292

Authors:

H.Yamaguchi,M.Matsushita,A.C.Nairn,J.Kuriyan

Key ref:

H.Yamaguchi et al. (2001). Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity. Mol Cell, 7, 1047-1057. PubMed id: 11389851 DOI: 10.1016/S1097-2765(01)00256-8

Date:

22-Mar-01 Release date: 06-Jun-01

Protein chains

Q923J1  (TRPM7_MOUSE) -  Transient receptor potential cation channel subfamily M member 7

Seq: 1863 a.a.

Struc: 253 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - Non-specific serine/threonine protein kinase.
• Reaction: ATP + a protein = ADP + a phosphoprotein

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

 Gene Ontology (GO) functional annotation 

• Biological process: protein amino acid phosphorylation (1 term)
• Biochemical function: protein serine/threonine kinase activity (2 terms)

reference

DOI no: 10.1016/S1097-2765(01)00256-8

Mol Cell 7:1047-1057 (2001)

PubMed id: 11389851

Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity.

H.Yamaguchi, M.Matsushita, A.C.Nairn, J.Kuriyan.

ABSTRACT

Transient receptor potential (TRP) channels modulate calcium levels in eukaryotic cells in response to external signals. A novel transient receptor potential channel has the ability to phosphorylate itself and other proteins on serine and threonine residues. The catalytic domain of this channel kinase has no detectable sequence similarity to classical eukaryotic protein kinases and is essential for channel function. The structure of the kinase domain, reported here, reveals unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains. The inclusion of the channel kinase catalytic domain within the eukaryotic protein kinase superfamily indicates a significantly wider distribution for this group of signaling proteins than suggested previously by sequence comparisons alone.

Selected figure(s)

Figure 6.
Figure 6. The Conserved GxG(A)xxG Motif in α-KinasesShown in red is the flexible loop (residues 1781–1799) that contains the conserved GxG(A)xxG motif in α-kinases. The Cα atoms of the glycine and alanine residues are shown in cyan (the C-terminal glycine is at the bottom). The substrate-mimicking peptide from PKA shown in green (Ala-17 in a yellow sphere) is docked to the ChaK molecular surface by superposing the ternary complex structure of PKA to the ChaK kinase domain. The AMP•PNP in the ChaK complex structure is also shown in the cleft

Figure 7.
Figure 7. Comparison of the Structural Platforms for the Catalytic Residues between ChaK and Its Structural NeighborsRibbon diagrams showing three β strands and four conserved residues in cAMP-dependent protein kinase, P. polycephalum actin-fragmin kinase (Protein Data Bank ID code 1cja; Steinbacher et al., 1999), ChaK, and E. coli succinyl-CoA synthetase. Strands in the N- and the C-terminal lobes are shown as yellow and green arrows, respectively. The protruding catalytic loops in PKA and actin-fragmin kinase as well as the corresponding segment in ChaK are colored in red. Conserved residues and the bound nucleotides are labeled

The above figures are reprinted by permission from Cell Press: Mol Cell (2001, 7, 1047-1057) copyright 2001.

Figures were selected by an automated process.