6WK5

Crystal structure of Gdx-Clo from Small Multidrug Resistance family of transporters

Summary for 6WK5

• Entry DOI: 10.2210/pdb6wk5/pdb
• Descriptor: Multidrug resistance protein, SMR family, L10 monobody (2 entities in total)
• Functional Keywords: small multidrug resistance, guanidinium transporter, emre homologue, dual topology protein, transport protein
• Biological source: Clostridiales bacterium oral taxon 876 str. F0540; More
• Total number of polymer chains: 4
• Total formula weight: 42922.76

Authors

Kermani, A.A.,Stockbridge, R.B. (deposition date: 2020-04-15, release date: 2020-10-28, Last modification date: 2024-10-30)

Primary citation

Kermani, A.A.,Macdonald, C.B.,Burata, O.E.,Ben Koff, B.,Koide, A.,Denbaum, E.,Koide, S.,Stockbridge, R.B.
The structural basis of promiscuity in small multidrug resistance transporters.
Nat Commun, 11:6064-6064, 2020

PubMed Abstract: By providing broad resistance to environmental biocides, transporters from the small multidrug resistance (SMR) family drive the spread of multidrug resistance cassettes among bacterial populations. A fundamental understanding of substrate selectivity by SMR transporters is needed to identify the types of selective pressures that contribute to this process. Using solid-supported membrane electrophysiology, we find that promiscuous transport of hydrophobic substituted cations is a general feature of SMR transporters. To understand the molecular basis for promiscuity, we solved X-ray crystal structures of a SMR transporter Gdx-Clo in complex with substrates to a maximum resolution of 2.3 Å. These structures confirm the family's extremely rare dual topology architecture and reveal a cleft between two helices that provides accommodation in the membrane for the hydrophobic substituents of transported drug-like cations.

PubMed: 33247110
DOI: 10.1038/s41467-020-19820-8

Experimental method

X-RAY DIFFRACTION (3.5 Å)