1JKK

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

Summary for 1JKK

• Entry DOI: 10.2210/pdb1jkk/pdb
• Descriptor: DEATH-ASSOCIATED PROTEIN KINASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P53355
• Total number of polymer chains: 1
• Total formula weight: 34324.87

Authors

Tereshko, V.,Teplova, M.,Brunzelle, J.,Watterson, D.M.,Egli, M. (deposition date: 2001-07-12, release date: 2002-04-01, Last modification date: 2024-02-07)

Primary citation

Tereshko, V.,Teplova, M.,Brunzelle, J.,Watterson, D.M.,Egli, M.
Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression.
Nat.Struct.Biol., 8:899-907, 2001

PubMed 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.

PubMed: 11573098
DOI: 10.1038/nsb1001-899

Experimental method

X-RAY DIFFRACTION (2.4 Å)