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.
Keywords:
structure; α-actinin.
© 2016 Wiley Periodicals, Inc.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actin Cytoskeleton / chemistry
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Actin Cytoskeleton / metabolism
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Actinin / chemistry*
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Actinin / genetics
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Actinin / metabolism
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Amino Acid Sequence
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Calcium / chemistry*
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Calcium / metabolism
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Calmodulin / chemistry*
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Calmodulin / genetics
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Calmodulin / metabolism
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Cloning, Molecular
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Entamoeba histolytica / chemistry*
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Entamoeba histolytica / genetics
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Entamoeba histolytica / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular
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Protein Binding
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Protein Folding
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Protein Interaction Domains and Motifs
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Protein Structure, Secondary
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Protozoan Proteins / chemistry*
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Protozoan Proteins / genetics
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Protozoan Proteins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Alignment
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Virulence Factors / chemistry*
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Virulence Factors / genetics
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Virulence Factors / metabolism
Substances
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Calmodulin
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Protozoan Proteins
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Recombinant Proteins
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Virulence Factors
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Actinin
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Calcium