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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.

Pubmed ID: 12351846


  • Terrak M
  • Otterbein LR
  • Wu G
  • Palecanda LA
  • Lu RC
  • Dominguez R


Acta crystallographica. Section D, Biological crystallography

Publication Data

October 27, 2002

Associated Grants

  • Agency: NIAMS NIH HHS, Id: R01 AR046524
  • Agency: NIAMS NIH HHS, Id: R01 AR46524
  • Agency: NCRR NIH HHS, Id: RR-01646
  • Agency: NCRR NIH HHS, Id: RR07707

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