The molecular basis of phosphite and hypophosphite recognition by ABC-transporters

Some bacteria can use inorganic phosphite and hypophosphite as sources of inorganic phosphorus. Here, the authors report crystal structures of the periplasmic proteins that bind these reduced phosphorus species and show that a P-H…π interaction between the ligand and binding site determines their sp...

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Main Authors:	Claudine Bisson, Nathan B. P. Adams, Ben Stevenson, Amanda A. Brindley, Despo Polyviou, Thomas S. Bibby, Patrick J. Baker, C. Neil Hunter, Andrew Hitchcock
Format:	Article
Language:	English
Published:	Nature Publishing Group 2017-11-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-01226-8

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spelling	doaj-fb628c898a23417e81de94e06a9805042021-05-11T07:31:08ZengNature Publishing GroupNature Communications2041-17232017-11-018111310.1038/s41467-017-01226-8The molecular basis of phosphite and hypophosphite recognition by ABC-transportersClaudine Bisson0Nathan B. P. Adams1Ben Stevenson2Amanda A. Brindley3Despo Polyviou4Thomas S. Bibby5Patrick J. Baker6C. Neil Hunter7Andrew Hitchcock8Department of Molecular Biology and Biotechnology, University of SheffieldDepartment of Molecular Biology and Biotechnology, University of SheffieldDepartment of Molecular Biology and Biotechnology, University of SheffieldDepartment of Molecular Biology and Biotechnology, University of SheffieldOcean and Earth Sciences, National Oceanography Centre Southampton, University of SouthamptonOcean and Earth Sciences, National Oceanography Centre Southampton, University of SouthamptonDepartment of Molecular Biology and Biotechnology, University of SheffieldDepartment of Molecular Biology and Biotechnology, University of SheffieldDepartment of Molecular Biology and Biotechnology, University of SheffieldSome bacteria can use inorganic phosphite and hypophosphite as sources of inorganic phosphorus. Here, the authors report crystal structures of the periplasmic proteins that bind these reduced phosphorus species and show that a P-H…π interaction between the ligand and binding site determines their specificity.https://doi.org/10.1038/s41467-017-01226-8
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Claudine Bisson Nathan B. P. Adams Ben Stevenson Amanda A. Brindley Despo Polyviou Thomas S. Bibby Patrick J. Baker C. Neil Hunter Andrew Hitchcock
spellingShingle	Claudine Bisson Nathan B. P. Adams Ben Stevenson Amanda A. Brindley Despo Polyviou Thomas S. Bibby Patrick J. Baker C. Neil Hunter Andrew Hitchcock The molecular basis of phosphite and hypophosphite recognition by ABC-transporters Nature Communications
author_facet	Claudine Bisson Nathan B. P. Adams Ben Stevenson Amanda A. Brindley Despo Polyviou Thomas S. Bibby Patrick J. Baker C. Neil Hunter Andrew Hitchcock
author_sort	Claudine Bisson
title	The molecular basis of phosphite and hypophosphite recognition by ABC-transporters
title_short	The molecular basis of phosphite and hypophosphite recognition by ABC-transporters
title_full	The molecular basis of phosphite and hypophosphite recognition by ABC-transporters
title_fullStr	The molecular basis of phosphite and hypophosphite recognition by ABC-transporters
title_full_unstemmed	The molecular basis of phosphite and hypophosphite recognition by ABC-transporters
title_sort	molecular basis of phosphite and hypophosphite recognition by abc-transporters
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2017-11-01
description	Some bacteria can use inorganic phosphite and hypophosphite as sources of inorganic phosphorus. Here, the authors report crystal structures of the periplasmic proteins that bind these reduced phosphorus species and show that a P-H…π interaction between the ligand and binding site determines their specificity.
url	https://doi.org/10.1038/s41467-017-01226-8
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The molecular basis of phosphite and hypophosphite recognition by ABC-transporters

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