1cja

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==ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM==
==ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM==
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<StructureSection load='1cja' size='340' side='right' caption='[[1cja]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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<StructureSection load='1cja' size='340' side='right'caption='[[1cja]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1cja]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1cja]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cja OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cja RCSB], [http://www.ebi.ac.uk/pdbsum/1cja PDBsum]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cja OCA], [https://pdbe.org/1cja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cja RCSB], [https://www.ebi.ac.uk/pdbsum/1cja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cja ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AFK_PHYPO AFK_PHYPO]] Has a role in the regulation of microfilament formation. Phosphorylates the actin-fragmin complex on threonine residues, in vitro.<ref>PMID:8896448</ref> <ref>PMID:1587799</ref> <ref>PMID:1315751</ref>
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[https://www.uniprot.org/uniprot/AFK_PHYPO AFK_PHYPO] Has a role in the regulation of microfilament formation. Phosphorylates the actin-fragmin complex on threonine residues, in vitro.<ref>PMID:8896448</ref> <ref>PMID:1587799</ref> <ref>PMID:1315751</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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:10357805<ref>PMID:10357805</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Physarum polycephalum]]
[[Category: Physarum polycephalum]]
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[[Category: Benz, J]]
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[[Category: Benz J]]
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[[Category: Eichinger, L]]
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[[Category: Eichinger L]]
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[[Category: Gettemans, J]]
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[[Category: Gettemans J]]
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[[Category: Hof, P]]
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[[Category: Hof P]]
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[[Category: Huber, R]]
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[[Category: Huber R]]
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[[Category: Schleicher, M]]
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[[Category: Schleicher M]]
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[[Category: Steinbacher, S]]
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[[Category: Steinbacher S]]
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[[Category: Vandekerckhove, J]]
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[[Category: Vandekerckhove J]]
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[[Category: Actin]]
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[[Category: Kinase]]
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[[Category: Transferase]]
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Current revision

ACTIN-FRAGMIN KINASE, CATALYTIC DOMAIN FROM PHYSARUM POLYCEPHALUM

PDB ID 1cja

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