2FCE

Solution structure of C-lobe Myosin Light Chain from Saccharomices cerevisiae

2FCE の概要

• エントリーDOI: 10.2210/pdb2fce/pdb
• 分子名称: Myosin light chain 1 (1 entity in total)
• 機能のキーワード: ef-hand protein, cell cycle
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Bud neck: P53141
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7897.89

構造登録者

Cicero, D.O.,Pennestri, M.,Contessa, G.M.,Paci, M.,Ragnini-Wilson, A.,Melino, S. (登録日: 2005-12-12, 公開日: 2006-11-07, 最終更新日: 2024-05-29)

主引用文献

Pennestri, M.,Melino, S.,Contessa, G.M.,Casavola, E.C.,Paci, M.,Ragnini-Wilson, A.,Cicero, D.O.
Structural basis for the interaction of the myosin light chain Mlc1p with the myosin V Myo2p IQ motifs.
J.Biol.Chem., 282:667-679, 2007

PubMed Abstract: Calmodulin, regulatory, and essential myosin light chain are evolutionary conserved proteins that, by binding to IQ motifs of target proteins, regulate essential intracellular processes among which are efficiency of secretory vesicles release at synapsis, intracellular signaling, and regulation of cell division. The yeast Saccharomyces cerevisiae calmodulin Cmd1 and the essential myosin light chain Mlc1p share the ability to interact with the class V myosin Myo2p and Myo4 and the class II myosin Myo1p. These myosins are required for vesicle, organelle, and mRNA transport, spindle orientation, and cytokinesis. We have used the budding yeast model system to study how calmodulin and essential myosin light chain selectively regulate class V myosin function. NMR structural analysis of uncomplexed Mlc1p and interaction studies with the first three IQ motifs of Myo2p show that the structural similarities between Mlc1p and the other members of the EF-hand superfamily of calmodulin-like proteins are mainly restricted to the C-lobe of these proteins. The N-lobe of Mlc1p presents a significantly compact and stable structure that is maintained both in the free and complexed states. The Mlc1p N-lobe interacts with the IQ motif in a manner that is regulated both by the IQ motifs sequence as well as by light chain structural features. These characteristic allows a distinctive interaction of Mlc1p with the first IQ motif of Myo2p when compared with calmodulin. This finding gives us a novel view of how calmodulin and essential light chain, through a differential binding to IQ1 of class V myosin motor, regulate this activity during vegetative growth and cytokinesis.

PubMed: 17074768
DOI: 10.1074/jbc.M607016200

実験手法

SOLUTION NMR