PDBsum entry 1jkt

Transferase

PDB id: 1jkt

Contents

Protein chains

276 a.a. *

* Residue conservation analysis

PDB id:

1jkt

Name:

Transferase

Title:

Tetragonal crystal form of a catalytic domain of death-associated protein kinase

Structure:

Death-associated protein kinase. Chain: a, b. Fragment: catalytic domain, protein kinase domain. Synonym: dap kinase 1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

3.50Å R-factor: 0.273 R-free: 0.297

Authors:

V.Tereshko,M.Teplova,J.Brunzelle,D.M.Watterson,M.Egli

Key ref:

V.Tereshko et al. (2001). Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression. Nat Struct Biol, 8, 899-907. PubMed id: 11573098 DOI: 10.1038/nsb1001-899

Date:

13-Jul-01 Release date: 01-Apr-02

Protein chains

P53355  (DAPK1_HUMAN) -  Death-associated protein kinase 1 from Homo sapiens

Seq: 1430 a.a.

Struc: 276 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine 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⁺

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

reference

DOI no: 10.1038/nsb1001-899

Nat Struct Biol 8:899-907 (2001)

PubMed id: 11573098

Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression.

V.Tereshko, M.Teplova, J.Brunzelle, D.M.Watterson, M.Egli.

ABSTRACT

We have determined X-ray crystal structures with up to 1.5 A resolution of the catalytic domain of death-associated protein kinase (DAPK), the first described member of a novel family of pro-apoptotic and tumor-suppressive serine/threonine kinases. The geometry of the active site was studied in the apo form, in a complex with nonhydrolyzable AMPPnP and in a ternary complex consisting of kinase, AMPPnP and either Mg2+ or Mn2+. The structures revealed a previously undescribed water-mediated stabilization of the interaction between the lysine that is conserved in protein kinases and the beta- and gamma-phosphates of ATP, as well as conformational changes at the active site upon ion binding. Comparison between these structures and nucleotide triphosphate complexes of several other kinases disclosed a number of unique features of the DAPK catalytic domain, among which is a highly ordered basic loop in the N-terminal domain that may participate in enzyme regulation.

Selected figure(s)

Figure 1.
Figure 1. Domain organization of DAPK (numbers refer to amino acids).

Figure 5.
Figure 5. Lattice interactions in the orthorhombic and cubic crystal forms of the DAPK catalytic domain. a, Orthorhombic form. Overview of the environment of the putative peptide-binding region preceding the F-helix and the basic loop linking 3 and helix C. Three symmetry mates colored blue, pink and cyan make up the immediate surroundings of the loop region of each DAPK molecule (red). Secondary structure elements are represented as cylinders and arrows, and AMPPnP molecules and four residues of the C-terminal streptavidin-tag visible in the electron density maps are in a ball-and-stick representation. b, Cubic form. The crystallographic asymmetric unit consists of DAPK dimers related by a noncrystallographic two-fold rotation axis running approximately along the vertical in the plane of projection. Thus, basic loops and peptide binding regions of the two molecules face each other.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2001, 8, 899-907) copyright 2001.

Figures were selected by an automated process.