ArticleThe EMBO journal1999
The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 36 citations in OpenAlex.
- Hyperosmotic stress-induced microtubule disassembly in Chlamydomonas reinhardtii.BMC plant biology · 2022Article
- The Physarum polycephalum Genome Reveals Extensive Use of Prokaryotic Two-Component and Metazoan-Type Tyrosine Kinase Signaling.Genome biology and evolution · 2015Article
- Crystal structure of the Golgi casein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Identification of a hidden strain switch provides clues to an ancient structural mechanism in protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Design principles underpinning the regulatory diversity of protein kinases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- A novel protein kinase-like domain in a selenoprotein, widespread in the tree of life.PloS one · 2012Article
- AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis.Nature chemical biology · 2009Article
- Structural and functional diversity of the microbial kinome.PLoS biology · 2007Article
- Structural evolution of the protein kinase-like superfamily.PLoS computational biology · 2005Article
- Overview of protein structural and functional folds.Current protocols in protein science · 2004Review
- Villidin, a novel WD-repeat and villin-related protein from Dictyostelium, is associated with membranes and the cytoskeleton.Molecular biology of the cell · 2003Article
- The retinitis pigmentosa GTPase regulator (RPGR)- interacting protein: subserving RPGR function and participating in disk morphogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Human members of the eukaryotic protein kinase family.Genome biology · 2002Article
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8 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
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.
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