2X0G

X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX

Summary for 2X0G

• Entry DOI: 10.2210/pdb2x0g/pdb
• Related: 1AJI 1CDL 1CLL 1CTR 1IG1 1IWQ 1J7O 1J7P 1JKK 1JKL 1JKS 1JKT 1K90 1K93 1LVC 1NKF 1P4F 1PK0 1S26 1SK6 1SW8 1WRZ 1XFU 1XFV 1XFW 1XFX 1XFY 1XFZ 1Y6W 1YRT 1YRU 1ZOT 2BE6 2F3Y 2F3Z 2V01 2V02 2VAY 2W4J 2W4K 2W73 2WEL
• Descriptor: DEATH-ASSOCIATED PROTEIN KINASE 1, CALMODULIN, SULFATE ION, ... (5 entities in total)
• Functional Keywords: transferase-signaling protein complex, transferase signaling protein complex, phosphoprotein, calmodulin-binding, dapk, kinase, ank repeat, calmodulin, transferase, atp-binding, transferase/signaling protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: P53355; Cytoplasm, cytoskeleton, spindle: P62158
• Total number of polymer chains: 2
• Total formula weight: 55527.87

Authors

Kuper, J.,De Diego, I.,Lehmann, F.,Wilmanns, M. (deposition date: 2009-12-08, release date: 2010-01-26, Last modification date: 2023-12-20)

Primary citation

De Diego, I.,Kuper, J.,Bakalova, N.,Kursula, P.,Wilmanns, M.
Molecular Basis of the Death-Associated Protein Kinase-Calcium/Calmodulin Regulator Complex.
Sci.Signal, 3:RA6-, 2010

PubMed Abstract: Death-associated protein kinase (DAPK) provides a model for calcium-bound calmodulin (CaM)-dependent protein kinases (CaMKs). Here, we report the crystal structure of the binary DAPK-CaM complex, using a construct that includes the DAPK catalytic domain and adjacent autoregulatory domain. When DAPK was in a complex with CaM, the DAPK autoregulatory domain formed a long seven-turn helix. This DAPK-CaM module interacted with the DAPK catalytic domain through two separate domain-domain interfaces, which involved the upper and the lower lobe of the catalytic domain. When bound to DAPK, CaM adopted an extended conformation, which was different from that in CaM-CaMK peptide complexes. Complementary biochemical analysis showed that the ability of DAPK to bind CaM correlated with its catalytic activity. Because many features of CaM binding are conserved in other CaMKs, our findings likely provide a generally applicable model for regulation of CaMK activity.

PubMed: 20103772
DOI: 10.1126/SCISIGNAL.2000552

Experimental method

X-RAY DIFFRACTION (2.2 Å)