title: Solution structure of the calmodulin-like C-terminal domain of Entamoeba α-actinin2.
abstract: Cell motility is dependent on a dynamic meshwork of actin filaments that is remodelled continuously. A large number of associated proteins that are severs, cross-links, or caps the filament ends have been identified and the actin cross-linker α-actinin has been implied in several important cellular processes. In Entamoeba histolytica, the etiological agent of human amoebiasis, α-actinin is believed to be required for infection. To better understand the role of α-actinin in the infectious process we have determined the solution structure of the C-terminal calmodulin-like domain using NMR. The final structure ensemble of the apo form shows two lobes, that both resemble other pairs of calcium-binding EF-hand motifs, connected with a mobile linker.
authors.affiliation: Swedish NMR Centre at the University of Gothenburg, PO Box 465, Gothenburg, SE-40530, Sweden.
authors.forename: Göran
authors.initials: G
authors.lastname: Karlsson
authors.affiliation: Swedish NMR Centre at the University of Gothenburg, PO Box 465, Gothenburg, SE-40530, Sweden.
authors.forename: Cecilia
authors.initials: C
authors.lastname: Persson
authors.affiliation: Swedish NMR Centre at the University of Gothenburg, PO Box 465, Gothenburg, SE-40530, Sweden.
authors.forename: Maxim
authors.initials: M
authors.lastname: Mayzel
authors.affiliation: Department of Chemistry, Umeå University, Umeå, SE-901 87, Sweden.
authors.forename: Mattias
authors.initials: M
authors.lastname: Hedenström
authors.affiliation: Department of Chemistry, Umeå University, Umeå, SE-901 87, Sweden.
authors.forename: Lars
authors.initials: L
authors.lastname: Backman
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000378:metabolism; D000185:Actinin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism; D002147:Calmodulin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D004748:Entamoeba histolytica / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D037521:Virulence Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D002147:Calmodulin; D015800:Protozoan Proteins; D011994:Recombinant Proteins; D037521:Virulence Factors; D000185:Actinin; D002118:Calcium
keywords: structure; α-actinin