title: Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V.
abstract: 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: D000595:Amino Acid Sequence; D001665:Binding Sites; D002455:Cell Division; D003001:Cloning, Molecular; D004926:Escherichia coli; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018994:Myosin Light Chains / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D024701:Myosin Type V / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000254:growth & development / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: C113979:MLC1 protein, S cerevisiae; D018994:Myosin Light Chains; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D024701:Myosin Type V