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 an...

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Published in:Acta crystallographica. Section D, Biological crystallography. Vol. 58; no. 10-2; pp. 1882 - 1885
Main Authors: Terrak, Mohammed, Otterbein, Ludovic R., Wu, Guanming, Palecanda, Lakshmi A., Lu, Renne C., Dominguez, Roberto
Format: Journal Article Web Resource
Language:English
Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-10-2002
Blackwell Publishing
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Summary: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.
Bibliography:ark:/67375/WNG-D7X9DG71-3
istex:DCCAA570C9B2B1F20FDBF346C1220C50F6A99FDF
ArticleID:AYDPU0063
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
scopus-id:2-s2.0-0036793039
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902013951