学術雑誌論文

学術雑誌論文

text

Acta Crystallographica Section F: Structural Biology Communications. 2026, 82(3), p. 83-93

Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain

International Union of Crystallography

英語

text

2026-02-26

https://doi.org/10.1107/S2053230X26001202

Wang J., Tsutsumi K., Hirose M., et al. Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain. Acta Crystallographica Section F: Structural Biology Communications 82, 83 (2026); https://doi.org/10.1107/S2053230X26001202.

RND-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.

This article is licensed under a Creative Commons Attribution 4.0 International License.

104590

Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain

International Union of Crystallography

英語

2026-02-26

Acta Crystallographica Section F: Structural Biology Communications

82

3

83

93

https://doi.org/10.1107/S2053230X26001202

https://hdl.handle.net/11094/104590