Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities

Mechanosensitive channels respond to mechanical forces exerted on the cell membrane and play vital roles in regulating the chemical equilibrium within cells and their environment. High-resolution structural information is required to understand the gating mechanisms of mechanosensitive channels. Pro...

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Autores principales:	Claudio Catalano, Danya Ben-Hail, Weihua Qiu, Paul Blount, Amedee des Georges, Youzhong Guo
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	YnaI SMA2000 NCMN cryo-EM Mechanosensitive Channel Chemical technology TP1-1185 Chemical engineering TP155-156
Acceso en línea:	https://doaj.org/article/d6ef261896024b6c834f3ab697fff4a4
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spelling	oai:doaj.org-article:d6ef261896024b6c834f3ab697fff4a42021-11-25T18:19:47ZCryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities10.3390/membranes111108492077-0375https://doaj.org/article/d6ef261896024b6c834f3ab697fff4a42021-10-01T00:00:00Zhttps://www.mdpi.com/2077-0375/11/11/849https://doaj.org/toc/2077-0375Mechanosensitive channels respond to mechanical forces exerted on the cell membrane and play vital roles in regulating the chemical equilibrium within cells and their environment. High-resolution structural information is required to understand the gating mechanisms of mechanosensitive channels. Protein-lipid interactions are essential for the structural and functional integrity of mechanosensitive channels, but detergents cannot maintain the crucial native lipid environment for purified mechanosensitive channels. Recently, detergent-free systems have emerged as alternatives for membrane protein structural biology. This report shows that while membrane-active polymer, SMA2000, could retain some native cell membrane lipids on the transmembrane domain of the mechanosensitive-like YnaI channel, the complete structure of the transmembrane domain of YnaI was not resolved. This reveals a significant limitation of SMA2000 or similar membrane-active copolymers. This limitation may come from the heterogeneity of the polymers and nonspecific interactions between the polymers and the relatively large hydrophobic pockets within the transmembrane domain of YnaI. However, this limitation offers development opportunities for detergent-free technology for challenging membrane proteins.Claudio CatalanoDanya Ben-HailWeihua QiuPaul BlountAmedee des GeorgesYouzhong GuoMDPI AGarticleYnaISMA2000NCMNcryo-EMMechanosensitive ChannelChemical technologyTP1-1185Chemical engineeringTP155-156ENMembranes, Vol 11, Iss 849, p 849 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	YnaI SMA2000 NCMN cryo-EM Mechanosensitive Channel Chemical technology TP1-1185 Chemical engineering TP155-156
spellingShingle	YnaI SMA2000 NCMN cryo-EM Mechanosensitive Channel Chemical technology TP1-1185 Chemical engineering TP155-156 Claudio Catalano Danya Ben-Hail Weihua Qiu Paul Blount Amedee des Georges Youzhong Guo Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities
description	Mechanosensitive channels respond to mechanical forces exerted on the cell membrane and play vital roles in regulating the chemical equilibrium within cells and their environment. High-resolution structural information is required to understand the gating mechanisms of mechanosensitive channels. Protein-lipid interactions are essential for the structural and functional integrity of mechanosensitive channels, but detergents cannot maintain the crucial native lipid environment for purified mechanosensitive channels. Recently, detergent-free systems have emerged as alternatives for membrane protein structural biology. This report shows that while membrane-active polymer, SMA2000, could retain some native cell membrane lipids on the transmembrane domain of the mechanosensitive-like YnaI channel, the complete structure of the transmembrane domain of YnaI was not resolved. This reveals a significant limitation of SMA2000 or similar membrane-active copolymers. This limitation may come from the heterogeneity of the polymers and nonspecific interactions between the polymers and the relatively large hydrophobic pockets within the transmembrane domain of YnaI. However, this limitation offers development opportunities for detergent-free technology for challenging membrane proteins.
format	article
author	Claudio Catalano Danya Ben-Hail Weihua Qiu Paul Blount Amedee des Georges Youzhong Guo
author_facet	Claudio Catalano Danya Ben-Hail Weihua Qiu Paul Blount Amedee des Georges Youzhong Guo
author_sort	Claudio Catalano
title	Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities
title_short	Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities
title_full	Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities
title_fullStr	Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities
title_full_unstemmed	Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities
title_sort	cryo-em structure of mechanosensitive channel ynai using sma2000: challenges and opportunities
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/d6ef261896024b6c834f3ab697fff4a4
work_keys_str_mv	AT claudiocatalano cryoemstructureofmechanosensitivechannelynaiusingsma2000challengesandopportunities AT danyabenhail cryoemstructureofmechanosensitivechannelynaiusingsma2000challengesandopportunities AT weihuaqiu cryoemstructureofmechanosensitivechannelynaiusingsma2000challengesandopportunities AT paulblount cryoemstructureofmechanosensitivechannelynaiusingsma2000challengesandopportunities AT amedeedesgeorges cryoemstructureofmechanosensitivechannelynaiusingsma2000challengesandopportunities AT youzhongguo cryoemstructureofmechanosensitivechannelynaiusingsma2000challengesandopportunities
_version_	1718411349241888768

Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities

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