22xk
From Proteopedia
Structural highlights
Publication Abstract from PubMedRND-type multidrug-efflux pumps are major contributors to multidrug resistance in Gram-negative bacteria, with MexY from Pseudomonas aeruginosa playing a central role in aminoglycoside resistance. Unlike other RND transporters, MexY exhibits unusually large open clefts in the binding and extrusion states. To determine whether this feature is intrinsic to its drug-recognition porter domain, we created a chimeric protein, MexBYB, by replacing the funnel-like and transmembrane domains of MexY with those of the homologous transporter MexB, and determined its structures by cryoEM under apo and kanamycin-supplemented conditions. Under both conditions, MexBYB was reported to adopt symmetric-like and asymmetric conformations. Structural comparisons reveal that the unusually large open clefts are retained in MexBYB, indicating that this feature is intrinsic to the MexY porter domain. Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain.,Wang J, Tsutsumi K, Hirose M, Nakashima R, Kato T, Nishino K, Nakagawa A, Yamashita E Acta Crystallogr F Struct Biol Commun. 2026 Mar 1;82(Pt 3):83-93. doi: , 10.1107/S2053230X26001202. Epub 2026 Feb 26. PMID:41744473[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
This page was last modified 08:53, 11 March 2026.