Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V.
Mlc1p is a calmodulin-like protein from the budding yeast Saccharomyces cerevisiae, where it has been identified as a subunit of a class V myosin, Myo2p, and a binding partner of an IQGAP-like protein, Iqg1p. Through its interactions with these two proteins, Mlc1p plays a role in polarized growth and cytokinesis. ... Mlc1p has been crystallized in complexes with four different IQ target motifs from the neck region of Myo2p: IQ2, IQ3, IQ4 and IQ2-IQ3 (referred to as IQ2,3). Electron-density maps for two of the complexes (Mlc1p-IQ4 and Mlc1p-IQ2,3) were obtained from multiple anomalous dispersion (MAD) experiments based on selenomethionine derivatives. The other two structures (Mlc1p-IQ2 and Mlc1p-IQ3) were determined by molecular replacement using the partially refined structure of Mlc1p-IQ2,3 as a search model.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Cell Division, Cloning, Molecular, Escherichia coli, Models, Molecular, Molecular Sequence Data, Myosin Light Chains, Myosin Type V, Protein Conformation, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, X-Ray Diffraction
Amino Acid Sequence, Binding Sites, Cell Division, Cloning, Molecular, Escherichia coli, Models, Molecular, Molecular Sequence Data, Myosin Light Chains, Myosin Type V, Protein Conformation, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, X-Ray Diffraction
Acta Crystallogr. D Biol. Crystallogr.
Date: Oct. 01, 2002
PubMed ID: 12351846
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