1CJA

ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM

Summary for 1CJA

• Entry DOI: 10.2210/pdb1cja/pdb
• Descriptor: PROTEIN (ACTIN-FRAGMIN KINASE), ADENOSINE MONOPHOSPHATE (2 entities in total)
• Functional Keywords: kinase, actin, transferase
• Biological source: Physarum polycephalum
• Total number of polymer chains: 2
• Total formula weight: 76893.57

Authors

Steinbacher, S.,Hof, P.,Eichinger, L.,Schleicher, M.,Gettemans, J.,Vandekerckhove, J.,Huber, R.,Benz, J. (deposition date: 1999-04-08, release date: 1999-06-18, Last modification date: 2024-02-07)

Primary citation

Steinbacher, S.,Hof, P.,Eichinger, L.,Schleicher, M.,Gettemans, J.,Vandekerckhove, J.,Huber, R.,Benz, J.
The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain.
EMBO J., 18:2923-2929, 1999

PubMed Abstract: Coordinated temporal and spatial regulation of the actin cytoskeleton is essential for diverse cellular processes such as cell division, cell motility and the formation and maintenance of specialized structures in differentiated cells. In plasmodia of Physarum polycephalum, the F-actin capping activity of the actin-fragmin complex is regulated by the phosphorylation of actin. This is mediated by a novel type of protein kinase with no sequence homology to eukaryotic-type protein kinases. Here we present the crystal structure of the catalytic domain of the first cloned actin kinase in complex with AMP at 2.9 A resolution. The three-dimensional fold reveals a catalytic module of approximately 160 residues, in common with the eukaryotic protein kinase superfamily, which harbours the nucleotide binding site and the catalytic apparatus in an inter-lobe cleft. Several kinases that share this catalytic module differ in the overall architecture of their substrate recognition domain. The actin-fragmin kinase has acquired a unique flat substrate recognition domain which is supposed to confer stringent substrate specificity.

PubMed: 10357805
DOI: 10.1093/emboj/18.11.2923

Experimental method

X-RAY DIFFRACTION (2.9 Å)