Structural highlights
Publication Abstract from PubMed
Transporters play vital roles in acquiring antimicrobial resistance among pathogenic bacteria. In this study, we report the X-ray structure of NorC, a 14-transmembrane major facilitator superfamily member that is implicated in fluoroquinolone resistance in drug-resistant Staphylococcus aureus strains, at a resolution of 3.6 A. The NorC structure was determined in complex with a single-domain camelid antibody that interacts at the extracellular face of the transporter and stabilizes it in an outward-open conformation. The complementarity determining regions of the antibody enter and block solvent access to the interior of the vestibule, thereby inhibiting alternating-access. NorC specifically interacts with an organic cation, tetraphenylphosphonium, although it does not demonstrate an ability to transport it. The interaction is compromised in the presence of NorC-antibody complex, consequently establishing a strategy to detect and block NorC and related transporters through the use of single-domain camelid antibodies.
Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody.,Kumar S, Athreya A, Gulati A, Nair RM, Mahendran I, Ranjan R, Penmatsa A Commun Biol. 2021 Jul 5;4(1):836. doi: 10.1038/s42003-021-02357-x. PMID:34226658[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kumar S, Athreya A, Gulati A, Nair RM, Mahendran I, Ranjan R, Penmatsa A. Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody. Commun Biol. 2021 Jul 5;4(1):836. PMID:34226658 doi:10.1038/s42003-021-02357-x
