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

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...

Full description

Bibliographic Details
Main Authors: Sushant Kumar, Arunabh Athreya, Ashutosh Gulati, Rahul Mony Nair, Ithayaraja Mahendran, Rakesh Ranjan, Aravind Penmatsa
Format: Article
Language:English
Published: Nature Publishing Group 2021-07-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-021-02357-x
id doaj-c16c7af762f549619faaeddc0375f262
record_format Article
spelling doaj-c16c7af762f549619faaeddc0375f2622021-07-11T11:13:31ZengNature Publishing GroupCommunications Biology2399-36422021-07-014111110.1038/s42003-021-02357-xStructural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibodySushant Kumar0Arunabh Athreya1Ashutosh Gulati2Rahul Mony Nair3Ithayaraja Mahendran4Rakesh Ranjan5Aravind Penmatsa6Molecular Biophysics Unit, Indian Institute of ScienceMolecular Biophysics Unit, Indian Institute of ScienceMolecular Biophysics Unit, Indian Institute of ScienceMolecular Biophysics Unit, Indian Institute of ScienceMolecular Biophysics Unit, Indian Institute of SciencePrincipal Scientist, ICAR-National Research Centre of Camel (NRCC)Molecular Biophysics Unit, Indian Institute of ScienceSushant 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.https://doi.org/10.1038/s42003-021-02357-x
collection DOAJ
language English
format Article
sources DOAJ
author Sushant Kumar
Arunabh Athreya
Ashutosh Gulati
Rahul Mony Nair
Ithayaraja Mahendran
Rakesh Ranjan
Aravind Penmatsa
spellingShingle 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
Communications Biology
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 Publishing Group
series Communications Biology
issn 2399-3642
publishDate 2021-07-01
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.
url https://doi.org/10.1038/s42003-021-02357-x
work_keys_str_mv AT sushantkumar structuralbasisofinhibitionofatransporterfromstaphylococcusaureusnorcthroughasingledomaincamelidantibody
AT arunabhathreya structuralbasisofinhibitionofatransporterfromstaphylococcusaureusnorcthroughasingledomaincamelidantibody
AT ashutoshgulati structuralbasisofinhibitionofatransporterfromstaphylococcusaureusnorcthroughasingledomaincamelidantibody
AT rahulmonynair structuralbasisofinhibitionofatransporterfromstaphylococcusaureusnorcthroughasingledomaincamelidantibody
AT ithayarajamahendran structuralbasisofinhibitionofatransporterfromstaphylococcusaureusnorcthroughasingledomaincamelidantibody
AT rakeshranjan structuralbasisofinhibitionofatransporterfromstaphylococcusaureusnorcthroughasingledomaincamelidantibody
AT aravindpenmatsa structuralbasisofinhibitionofatransporterfromstaphylococcusaureusnorcthroughasingledomaincamelidantibody
_version_ 1721309270485499904

Similar Items