Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1882-5. Epub 2002 Sep 28.

Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V.

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

Source

Boston Biomedical Research Institute, 64 Grove Street, Watertown, Massachusetts 02472, USA.

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.

PMID:: 12351846; [PubMed - indexed for MEDLINE]

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Cited by 3 PubMed Central articles

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Structures reported by this article

Ternary Complex Of Mlc1p Bound To Iq2 And Iq3 Of Myo2p, A Class V Myosinÿ

PDB: 1N2D

Source: Saccharomyces cerevisiae

Method: X-Ray Diffraction

Resolution: 2 Å

See all 3 structures...

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