7d5p

Structure of NorC transporter in an outward-open conformation in complex with a single-chain Indian camelid antibody

spinqualitylabelsall models 7d5p, resolution 3.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7d5p is a 4 chain structure with sequence from Camelus dromedarius and Staphylococcus aureus subsp. aureus COL. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.65Å Ligands: MSE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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