Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method

Electron paramagnetic resonance (EPR)-based hybrid experimental and computational approaches were applied to determine the structure of a full-length E. coli integral membrane sulfurtransferase, dimeric YgaP, and its structural and dynamic changes upon ligand binding. The solution NMR structures of...

Full description

Bibliographic Details
Main Authors:	Ling, Shenglong, Wang, Wei, Yu, Lu, Peng, Junhui, Cai, Xiaoying, Xiong, Ying, Hayati, Zahra, Zhang, Longhua, Zhang, Zhiyong, Song, Likai, Tian, Changlin
Format:	Online
Language:	English
Published:	Nature Publishing Group 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730233/

id	pubmed-4730233
recordtype	oai_dc
spelling	pubmed-47302332016-02-03 Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method Ling, Shenglong Wang, Wei Yu, Lu Peng, Junhui Cai, Xiaoying Xiong, Ying Hayati, Zahra Zhang, Longhua Zhang, Zhiyong Song, Likai Tian, Changlin Article Electron paramagnetic resonance (EPR)-based hybrid experimental and computational approaches were applied to determine the structure of a full-length E. coli integral membrane sulfurtransferase, dimeric YgaP, and its structural and dynamic changes upon ligand binding. The solution NMR structures of the YgaP transmembrane domain (TMD) and cytosolic catalytic rhodanese domain were reported recently, but the tertiary fold of full-length YgaP was not yet available. Here, systematic site-specific EPR analysis defined a helix-loop-helix secondary structure of the YagP-TMD monomers using mobility, accessibility and membrane immersion measurements. The tertiary folds of dimeric YgaP-TMD and full-length YgaP in detergent micelles were determined through inter- and intra-monomer distance mapping and rigid-body computation. Further EPR analysis demonstrated the tight packing of the two YgaP second transmembrane helices upon binding of the catalytic product SCN−, which provides insight into the thiocyanate exportation mechanism of YgaP in the E. coli membrane. Nature Publishing Group 2016-01-28 /pmc/articles/PMC4730233/ /pubmed/26817826 http://dx.doi.org/10.1038/srep20025 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Ling, Shenglong Wang, Wei Yu, Lu Peng, Junhui Cai, Xiaoying Xiong, Ying Hayati, Zahra Zhang, Longhua Zhang, Zhiyong Song, Likai Tian, Changlin
spellingShingle	Ling, Shenglong Wang, Wei Yu, Lu Peng, Junhui Cai, Xiaoying Xiong, Ying Hayati, Zahra Zhang, Longhua Zhang, Zhiyong Song, Likai Tian, Changlin Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method
author_facet	Ling, Shenglong Wang, Wei Yu, Lu Peng, Junhui Cai, Xiaoying Xiong, Ying Hayati, Zahra Zhang, Longhua Zhang, Zhiyong Song, Likai Tian, Changlin
author_sort	Ling, Shenglong
title	Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method
title_short	Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method
title_full	Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method
title_fullStr	Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method
title_full_unstemmed	Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method
title_sort	structure of an e. coli integral membrane sulfurtransferase and its structural transition upon scn− binding defined by epr-based hybrid method
description	Electron paramagnetic resonance (EPR)-based hybrid experimental and computational approaches were applied to determine the structure of a full-length E. coli integral membrane sulfurtransferase, dimeric YgaP, and its structural and dynamic changes upon ligand binding. The solution NMR structures of the YgaP transmembrane domain (TMD) and cytosolic catalytic rhodanese domain were reported recently, but the tertiary fold of full-length YgaP was not yet available. Here, systematic site-specific EPR analysis defined a helix-loop-helix secondary structure of the YagP-TMD monomers using mobility, accessibility and membrane immersion measurements. The tertiary folds of dimeric YgaP-TMD and full-length YgaP in detergent micelles were determined through inter- and intra-monomer distance mapping and rigid-body computation. Further EPR analysis demonstrated the tight packing of the two YgaP second transmembrane helices upon binding of the catalytic product SCN−, which provides insight into the thiocyanate exportation mechanism of YgaP in the E. coli membrane.
publisher	Nature Publishing Group
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730233/
_version_	1613529602229010432

Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN− binding defined by EPR-based hybrid method

Similar Items