Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody

Sushant Kumar et. al. report the 3.6 Å resolution crystal structure of NorC, a 14-transmembrane major facilitator superfamily member that is implicated in fluoroquinolone resistance in drug-resistant Staphylococcus aureus strains. The NorC structure was determined in complex with a single-domain cam...

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Autores principales:	Sushant Kumar, Arunabh Athreya, Ashutosh Gulati, Rahul Mony Nair, Ithayaraja Mahendran, Rakesh Ranjan, Aravind Penmatsa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c16c7af762f549619faaeddc0375f262
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spelling	oai:doaj.org-article:c16c7af762f549619faaeddc0375f2622021-12-02T15:22:55ZStructural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody10.1038/s42003-021-02357-x2399-3642https://doaj.org/article/c16c7af762f549619faaeddc0375f2622021-07-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02357-xhttps://doaj.org/toc/2399-3642Sushant Kumar et. al. report the 3.6 Å resolution crystal structure of NorC, a 14-transmembrane major facilitator superfamily member that is implicated in fluoroquinolone resistance in drug-resistant Staphylococcus aureus strains. The NorC structure was determined in complex with a single-domain camelid antibody that blocks access to the transporter and thus constitutes a new mode of inhibition.Sushant KumarArunabh AthreyaAshutosh GulatiRahul Mony NairIthayaraja MahendranRakesh RanjanAravind PenmatsaNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Sushant Kumar Arunabh Athreya Ashutosh Gulati Rahul Mony Nair Ithayaraja Mahendran Rakesh Ranjan Aravind Penmatsa Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody
description	Sushant Kumar et. al. report the 3.6 Å resolution crystal structure of NorC, a 14-transmembrane major facilitator superfamily member that is implicated in fluoroquinolone resistance in drug-resistant Staphylococcus aureus strains. The NorC structure was determined in complex with a single-domain camelid antibody that blocks access to the transporter and thus constitutes a new mode of inhibition.
format	article
author	Sushant Kumar Arunabh Athreya Ashutosh Gulati Rahul Mony Nair Ithayaraja Mahendran Rakesh Ranjan Aravind Penmatsa
author_facet	Sushant Kumar Arunabh Athreya Ashutosh Gulati Rahul Mony Nair Ithayaraja Mahendran Rakesh Ranjan Aravind Penmatsa
author_sort	Sushant Kumar
title	Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody
title_short	Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody
title_full	Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody
title_fullStr	Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody
title_full_unstemmed	Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody
title_sort	structural basis of inhibition of a transporter from staphylococcus aureus, norc, through a single-domain camelid antibody
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c16c7af762f549619faaeddc0375f262
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Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody

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