1cja
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(New page: 200px<br /><applet load="1cja" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cja, resolution 2.9Å" /> '''ACTIN-FRAGMIN KINASE,...)
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Revision as of 23:28, 24 November 2007
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ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM
Overview
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.
About this Structure
1CJA is a Single protein structure of sequence from Physarum polycephalum with AMP as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain., Steinbacher S, Hof P, Eichinger L, Schleicher M, Gettemans J, Vandekerckhove J, Huber R, Benz J, EMBO J. 1999 Jun 1;18(11):2923-9. PMID:10357805
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