| アイテムタイプ |
会議発表用資料 / Presentation(1) |
| 公開日 |
2025-08-20 |
| タイトル |
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|
タイトル |
Unveiling the photoactivation mechanism of photoactivated adenylate cyclase by hybrid molecular simulation |
|
言語 |
en |
| 言語 |
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|
言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6670 |
|
資源タイプ |
conference poster |
| 著者 |
Taguchi Masahiko
福田 諒哉
Sakuraba Shun
Wai Soon Chan
Nango Eriko
Kono Hidetoshi
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| 抄録 |
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内容記述 |
Photoactivated adenylate cyclase (PAC) directly synthesizes cAMP by light ac tivation. This unique photoswitch function is currently utilized as a new op togenetics tool. However, the free-energy profile of the photoisomerization reaction and how the structural changes in the photoreceptor domain propagate and control the catalytic domain have yet to be understood. First, we iden tified chemical structure of photoreceived region using a hybrid QM/MM free-energy method. Second, we performed MD simulation for full-length PAC using the optimized dark and light state geometries and charges around the chromophore. Analysis of the free-energy difference between the dark and light stat es indicates that the energy upon light reception is primarily stored in the surrounding environment, and only a small part of the total energy gain is stored in the photo-received region. This suggests that the protein structur e is essential to maintain the chemically unstable structure during the photoactive signaling state. We also clarified characteristic open and close movements at the interface between the photoreceptor and enzymatic domains in the light state. These results give molecular insight into the signal propagation mechanism of PAC upon photoactivation. |
| 会議概要（会議名, 開催地, 会期, 主催者等） |
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内容記述 |
第25回日本蛋白質科学会年会 |
| 発表年月日 |
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日付 |
2025-06-18 |
