Crystal structures of multidrug efflux transporters from Burkholderia pseudomallei suggest details of transport mechanism

Takaaki Kato, Ui Okada, Li Wei Hung, Eiki Yamashita, Heung Bok Kim, Chang Yub Kim, Thomas C. Terwilliger, Herbert P. Schweizer, Satoshi Murakami

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

BpeB and BpeF are multidrug efflux transporters from Burkholderia pseudomallei that enable multidrug resistance. Here, we report the crystal structures of BpeB and BpeF at 2.94 Å and 3.0 Å resolution, respectively. BpeB was found as an asymmetric trimer, consistent with the widely-accepted functional rotation mechanism for this type of transporter. One of the monomers has a distinct structure that we interpret as an intermediate along this functional cycle. Additionally, a detergent molecule bound in a previously undescribed binding site provides insights into substrate translocation through the pathway. BpeF shares structural similarities with the crystal structure of OqxB from Klebsiella pneumoniae, where both are symmetric trimers composed of three “binding”-state monomers. The structures of BpeB and BpeF further our understanding of the functional mechanisms of transporters belonging to the HAE1-RND superfamily.

Original languageEnglish (US)
Article numbere2215072120
JournalProceedings of the National Academy of Sciences of the United States of America
Volume120
Issue number29
DOIs
StatePublished - Jul 18 2023

ASJC Scopus subject areas

  • General

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