X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB

Guan and Hariharan report two crystal structures of melibiose transporter MelB in complex with substrate analogs, nitrophenyl-galactoside, and dodecyl-melibioside. Both structures revealed similar specific site for sugar recognition and resolved the cation-binding pocket, advancing the understanding...

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Autores principales:	Lan Guan, Parameswaran Hariharan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/4ed773bcbbe34592b3e96145426c9b47
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spelling	oai:doaj.org-article:4ed773bcbbe34592b3e96145426c9b472021-12-02T16:34:04ZX-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB10.1038/s42003-021-02462-x2399-3642https://doaj.org/article/4ed773bcbbe34592b3e96145426c9b472021-08-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02462-xhttps://doaj.org/toc/2399-3642Guan and Hariharan report two crystal structures of melibiose transporter MelB in complex with substrate analogs, nitrophenyl-galactoside, and dodecyl-melibioside. Both structures revealed similar specific site for sugar recognition and resolved the cation-binding pocket, advancing the understanding of MelB and related transporters.Lan GuanParameswaran HariharanNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Lan Guan Parameswaran Hariharan X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB
description	Guan and Hariharan report two crystal structures of melibiose transporter MelB in complex with substrate analogs, nitrophenyl-galactoside, and dodecyl-melibioside. Both structures revealed similar specific site for sugar recognition and resolved the cation-binding pocket, advancing the understanding of MelB and related transporters.
format	article
author	Lan Guan Parameswaran Hariharan
author_facet	Lan Guan Parameswaran Hariharan
author_sort	Lan Guan
title	X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB
title_short	X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB
title_full	X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB
title_fullStr	X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB
title_full_unstemmed	X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB
title_sort	x-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter melb
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/4ed773bcbbe34592b3e96145426c9b47
work_keys_str_mv	AT languan xraycrystallographyrevealsmolecularrecognitionmechanismforsugarbindinginamelibiosetransportermelb AT parameswaranhariharan xraycrystallographyrevealsmolecularrecognitionmechanismforsugarbindinginamelibiosetransportermelb
_version_	1718383750884098048

X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB

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