1cja

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[[Image:1cja.gif|left|200px]]<br /><applet load="1cja" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1cja.gif|left|200px]]
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caption="1cja, resolution 2.9&Aring;" />
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'''ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM'''<br />
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{{Structure
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|PDB= 1cja |SIZE=350|CAPTION= <scene name='initialview01'>1cja</scene>, resolution 2.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1CJA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJA OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10357805 10357805]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10357805 10357805]
[[Category: Physarum polycephalum]]
[[Category: Physarum polycephalum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: kinase]]
[[Category: kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:06 2008''

Revision as of 08:25, 20 March 2008


PDB ID 1cja

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



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. 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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