التفاصيل البيبلوغرافية
| العنوان: |
Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling. |
| المؤلفون: |
Lu, Qing1, Li, Jianchao1, Ye, Fei2, Zhang, Mingjie3 |
| المصدر: |
Nature Structural & Molecular Biology. Jan2015, Vol. 22 Issue 1, p81-88. 8p. |
| مصطلحات موضوعية: |
*MYOSIN, *CALMODULIN, *CRYSTAL structure, *MUSCLE proteins, *CALCIUM-binding proteins |
| مستخلص: |
Class I myosins can sense cellular mechanical forces and function as tension-sensitive anchors or transporters. How mechanical load is transduced from the membrane-binding tail to the force-generating head in myosin-1 is unknown. Here we determined the crystal structure of the entire tail of mouse myosin-1c in complex with apocalmodulin, showing that myosin-1c adopts a stable monomer conformation suited for force transduction. The lever-arm helix and the C-terminal extended PH domain of the motor are coupled by a stable post-IQ domain bound to calmodulin in a highly unusual mode. Ca2+ binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail. Our study provides a structural blueprint for the neck and tail domains of myosin-1 and expands the target binding modes of the master Ca2+-signal regulator calmodulin. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
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