1JKK : 2.4A X-RAY STRUCTURE OF TERNARY COMPLEX OF A CATALYTIC DOMAIN OF DEATH-ASSOCIATED PROTEIN KINASE WITH ATP ANALOGUE AND MG.

  • Daniel M Watterson (Contributor)
  • Joseph S. Brunzelle (Northwestern University, Argonne National Laboratory) (Contributor)
  • Valentina Tereshko (Contributor)
  • Marianna Teplova (Contributor)
  • Martin Egli (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.4
Classification:TRANSFERASE
Release Date:2002-04-01
Deposition Date:2001-07-12
Revision Date:2008-04-27#2011-07-13
Molecular Weight:34324.87
Macromolecule Type:Protein
Residue Count:294
Atom Site Count:2277
DOI:10.2210/pdb1jkk/pdb

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.
Date made available2002
PublisherRCSB-PDB

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