Structural insights into GABA transport inhibition using an engineered neurotransmitter transporter
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Joseph, Deepthi↗
Engineering topics
Penmatsa, Aravind
Publications and source records attributed to Penmatsa, Aravind.
Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody
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 Å. 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.
59 BASIC BIOLOGICAL SCIENCES↗
Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transpor
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Pidathala, Shabareesh↗