1cja
From Proteopedia
(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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| - | [[Image:1cja.gif|left|200px]]<br /><applet load="1cja" size=" | + | [[Image:1cja.gif|left|200px]]<br /><applet load="1cja" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cja, resolution 2.9Å" /> | caption="1cja, resolution 2.9Å" /> | ||
'''ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM'''<br /> | '''ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Coordinated temporal and spatial regulation of the actin cytoskeleton is | + | 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== | ==About this Structure== | ||
| - | 1CJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum] with AMP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum] with <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: kinase]] | [[Category: kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:41 2008'' |
Revision as of 10:06, 21 February 2008
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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 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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