1M45

CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ2 OF MYO2P, A CLASS V MYOSIN

1M45 の概要

• エントリーDOI: 10.2210/pdb1m45/pdb
• 関連するPDBエントリー: 1M46
• 分子名称: Myosin light chain, IQ2 Motif from MYO2P, A Class V Myosin (3 entities in total)
• 機能のキーワード: protein-peptide complex, iq motif, myosin light chain, cell cycle protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Bud neck: P53141 P19524
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19325.63

構造登録者

Terrak, M.,Dominguez, R. (登録日: 2002-07-02, 公開日: 2003-02-11, 最終更新日: 2024-02-14)

主引用文献

Terrak, M.,Wu, G.,Stafford, W.F.,Lu, R.C.,Dominguez, R.
Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications
Embo J., 22:362-371, 2003

PubMed Abstract: IQ motifs are widespread in nature. Mlc1p is a calmodulin-like myosin light chain that binds to IQ motifs of a class V myosin, Myo2p, and an IQGAP-related protein, Iqg1p, playing a role in polarized growth and cytokinesis in Saccharomyces cerevisiae. The crystal structures of Mlc1p bound to IQ2 and IQ4 of Myo2p differ dramatically. When bound to IQ2, Mlc1p adopts a compact conformation in which both the N- and C-lobes interact with the IQ motif. However, in the complex with IQ4, the N-lobe no longer interacts with the IQ motif, resulting in an extended conformation of Mlc1p. The two light chain structures relate to two distinct subfamilies of IQ motifs, one of which does not interact with the N-lobes of calmodulin-like light chains. The correlation between light chain structure and IQ sequence is demonstrated further by sedimentation velocity analysis of complexes of Mlc1p with IQ motifs from Myo2p and Iqg1p. The resulting 'free' N-lobes of myosin light chains in the extended conformation could mediate the formation of ternary complexes during protein localization and/or partner recruitment.

PubMed: 12554638
DOI: 10.1093/emboj/cdg058

実験手法

X-RAY DIFFRACTION (1.65 Å)