Reversible Molecular Motional Switch Based on Circular Photoactive Protein Oligomers: Unexpected Photo-Induced Contraction

Sang Jin Lee, Youngmin Kim, Tae Wu Kim, Cheolhee Yang, Kamatchi Thamilselvan, Hyeongseop Jeong, J. Hyun, H. Ihee
{"title":"Reversible Molecular Motional Switch Based on Circular Photoactive Protein Oligomers: Unexpected Photo-Induced Contraction","authors":"Sang Jin Lee, Youngmin Kim, Tae Wu Kim, Cheolhee Yang, Kamatchi Thamilselvan, Hyeongseop Jeong, J. Hyun, H. Ihee","doi":"10.2139/ssrn.3858909","DOIUrl":null,"url":null,"abstract":"Molecular switches alterable between two stable states by environmental stimuli such as light and temperature offer the potential for controlling biological functions. Here, we report a photoswitchable protein complex made of multiple protein molecules that can rapidly and reversibly switch with significant conformational changes. The structural and photochromic properties of photoactive yellow protein (PYP) are harnessed to construct circular oligomer PYPs (coPYPs) of desired sizes. Considering the light-induced N-terminal protrusion of monomer PYP, we expected coPYPs would expand upon irradiation, but time-resolved x-ray scattering data reveal that the late intermediate has a light-induced contraction motion. This work not only provides an approach to engineering a novel protein-based molecular switch based on circular oligomers of a well-known protein unit but also demonstrates the importance of actually characterizing the structural dynamics of designed molecular switches.","PeriodicalId":11894,"journal":{"name":"EngRN: Biomaterials (Topic)","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2021-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"EngRN: Biomaterials (Topic)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2139/ssrn.3858909","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Molecular switches alterable between two stable states by environmental stimuli such as light and temperature offer the potential for controlling biological functions. Here, we report a photoswitchable protein complex made of multiple protein molecules that can rapidly and reversibly switch with significant conformational changes. The structural and photochromic properties of photoactive yellow protein (PYP) are harnessed to construct circular oligomer PYPs (coPYPs) of desired sizes. Considering the light-induced N-terminal protrusion of monomer PYP, we expected coPYPs would expand upon irradiation, but time-resolved x-ray scattering data reveal that the late intermediate has a light-induced contraction motion. This work not only provides an approach to engineering a novel protein-based molecular switch based on circular oligomers of a well-known protein unit but also demonstrates the importance of actually characterizing the structural dynamics of designed molecular switches.
基于圆形光活性蛋白低聚物的可逆分子运动开关:意想不到的光诱导收缩
受环境刺激(如光和温度)在两种稳定状态之间变化的分子开关提供了控制生物功能的潜力。在这里,我们报道了一种由多个蛋白质分子组成的光切换蛋白复合物,它可以快速可逆地切换,并发生显著的构象变化。利用光活性黄蛋白(PYP)的结构和光致变色特性,构建了理想尺寸的环状低聚物PYPs (coPYPs)。考虑到单体PYP的光致n端突出,我们预计coPYPs会在照射后扩大,但时间分辨x射线散射数据显示,后期中间体有光致收缩运动。这项工作不仅提供了一种基于已知蛋白质单元的圆形低聚物的新型蛋白质分子开关的工程方法,而且还证明了实际表征设计的分子开关的结构动力学的重要性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信