title: Crystal structure of human coactosin-like protein.
abstract: Human coactosin-like protein is an actin filament binding protein but does not bind to globular actin. It associates with 5-Lipoxygenase both in vivo and in vitro, playing important roles in modulating the activities of actin and 5-Lipoxygenase. Coactosin counteracts the capping activity of capping protein which inhibits the actin polymerization. We determined the crystal structures of human coactosin-like protein by multi-wavelength anomalous dispersion method. The structure showed a high level of similarity to ADF-H domain, although their amino acid sequences share low degree of homology. A few conserved hydrophobic residues that may contribute to the folding were identified. This structure suggests coactosin-like protein bind to F-actin in a different way from ADF/Cofilin family. Combined with the information from previous mutagenesis studies, the binding sites for F-actin and 5-Lipoxygenase were analyzed, respectively. These two sites are quite close, which might prevent F-actin and 5-Lipoxygenase from binding to coactosin simultaneously.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
authors.forename: Lin
authors.initials: L
authors.lastname: Liu
authors.forename: Zhiyi
authors.initials: Z
authors.lastname: Wei
authors.forename: Yanli
authors.initials: Y
authors.lastname: Wang
authors.forename: Mao
authors.initials: M
authors.lastname: Wan
authors.forename: Zhongjun
authors.initials: Z
authors.lastname: Cheng
authors.forename: Weimin
authors.initials: W
authors.lastname: Gong
mesh_terms: D051339:Actin Depolymerizing Factors; D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D001094:Arachidonate 5-Lipoxygenase / Q000378:metabolism; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006639:Histidine / Q000737:chemistry; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D013058:Mass Spectrometry; D008715:Methionine / Q000737:chemistry; D008840:Microfilament Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000037:antagonists & inhibitors; D011485:Protein Binding; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012643:Selenium / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D014867:Water / Q000737:chemistry
chemical_list: D051339:Actin Depolymerizing Factors; D000199:Actins; C118115:COTL1 protein, human; D008840:Microfilament Proteins; D009687:Nuclear Proteins; D011994:Recombinant Proteins; D014867:Water; C066575:CAPG protein, human; D006639:Histidine; D008715:Methionine; D001094:Arachidonate 5-Lipoxygenase; D012643:Selenium