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

Sushant Kumar; Arunabh Athreya; Ashutosh Gulati; Rahul Mony Nair; Ithayaraja Mahendran; Rakesh Ranjan; Aravind Penmatsa

doi:10.1038/s42003-021-02357-x

Communications Biology (Jul 2021)

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

Sushant Kumar,
Arunabh Athreya,
Ashutosh Gulati,
Rahul Mony Nair,
Ithayaraja Mahendran,
Rakesh Ranjan,
Aravind Penmatsa

Affiliations

Sushant Kumar: Molecular Biophysics Unit, Indian Institute of Science
Arunabh Athreya: Molecular Biophysics Unit, Indian Institute of Science
Ashutosh Gulati: Molecular Biophysics Unit, Indian Institute of Science
Rahul Mony Nair: Molecular Biophysics Unit, Indian Institute of Science
Ithayaraja Mahendran: Molecular Biophysics Unit, Indian Institute of Science
Rakesh Ranjan: Principal Scientist, ICAR-National Research Centre of Camel (NRCC)
Aravind Penmatsa: Molecular Biophysics Unit, Indian Institute of Science

DOI: https://doi.org/10.1038/s42003-021-02357-x
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 11

Abstract

Read online

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.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

About the journal