Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.62
Classification:TRANSFERASE
Release Date:2002-04-01
Deposition Date:2001-07-12
Revision Date:2008-04-27#2011-07-13
Molecular Weight:34300.56
Macromolecule Type:Protein
Residue Count:294
Atom Site Count:2305
DOI:10.2210/pdb1jkl/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.
Resolution:1.62
Classification:TRANSFERASE
Release Date:2002-04-01
Deposition Date:2001-07-12
Revision Date:2008-04-27#2011-07-13
Molecular Weight:34300.56
Macromolecule Type:Protein
Residue Count:294
Atom Site Count:2305
DOI:10.2210/pdb1jkl/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 available | 2002 |
|---|---|
| Publisher | RCSB-PDB |