2015年9月
Calcium-controlled conformational choreography in the N-terminal half of adseverin
NATURE COMMUNICATIONS
- ,
- ,
- ,
- 巻
- 6
- 号
- 開始ページ
- 8254
- 終了ページ
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/ncomms9254
- 出版者・発行元
- NATURE PUBLISHING GROUP
Adseverin is a member of the calcium-regulated gelsolin superfamily of actin-binding proteins. Here we report the crystal structure of the calcium-free N-terminal half of adseverin (iA1-A3) and the Ca2+-bound structure of A3, which reveal structural similarities and differences with gelsolin. Solution small-angle X-ray scattering combined with ensemble optimization revealed a dynamic Ca2+-dependent equilibrium between inactive, intermediate and active conformations. Increasing calcium concentrations progressively shift this equilibrium from a main population of inactive conformation to the active form. Molecular dynamics simulations of iA1-A3 provided insights into Ca2+-induced destabilization, implicating a critical role for the A2 type II calcium-binding site and the A2A3 linker in the activation process. Finally, mutations that disrupt the A1/A3 interface increase Ca2+-independent F-actin severing by A1-A3, albeit at a lower efficiency than observed for gelsolin domains G1-G3. Together, these data address the calcium dependency of A1-A3 activity in relation to the calcium-independent activity of G1-G3.
- リンク情報
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- DOI
- https://doi.org/10.1038/ncomms9254
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/26365202
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000363017500025&DestApp=WOS_CPL
- URL
- http://orcid.org/0000-0001-6367-6903
- ID情報
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- DOI : 10.1038/ncomms9254
- ISSN : 2041-1723
- ORCIDのPut Code : 26727837
- PubMed ID : 26365202
- Web of Science ID : WOS:000363017500025