Reference : Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound t...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V
Terrak, Mohammed mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Otterbein, L. R. [> > > >]
Wu, G. [> > > >]
Palecanda, L. A. [> > > >]
Lu, R. C. [> > > >]
Dominguez, R. [> > > >]
Acta Crystallographica Section D-Biological Crystallography
Blackwell Publishing
Pt 10 Pt 2
Yes (verified by ORBi)
United Kingdom
[en] Amino Acid Sequence ; Binding Sites ; Cell Division ; Cloning, Molecular ; Escherichia coli ; Models, Molecular ; Molecular Sequence Data ; Myosin Light Chains/*chemistry/isolation & purification/metabolism ; Myosin Type V/*chemistry/metabolism ; Protein Conformation ; Recombinant Proteins/chemistry/isolation & purification/metabolism ; Saccharomyces cerevisiae/growth & development/physiology ; Saccharomyces cerevisiae Proteins/chemistry/isolation & ; purification/metabolism ; Support, U.S. Gov't, Non-P.H.S. ; Support, U.S. Gov't, P.H.S. ; X-Ray Diffraction/methods
[en] 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.

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