7WLV

Crystal Structure of the Multidrug effulx transporter BpeF from Burkholderia pseudomallei.

Summary for 7WLV

• Entry DOI: 10.2210/pdb7wlv/pdb
• Related: 7WLS
• Descriptor: Efflux pump membrane transporter, DODECYL-BETA-D-MALTOSIDE (3 entities in total)
• Functional Keywords: membrane protein, transport protein
• Biological source: Burkholderia pseudomallei K96243
• Total number of polymer chains: 6
• Total formula weight: 695106.93

Authors

Kato, T.,Hung, L.-W.,Yamashita, E.,Okada, U.,Terwilliger, T.C.,Murakami, S. (deposition date: 2022-01-13, release date: 2023-07-19, Last modification date: 2023-11-29)

Primary citation

Kato, T.,Okada, U.,Hung, L.W.,Yamashita, E.,Kim, H.B.,Kim, C.Y.,Terwilliger, T.C.,Schweizer, H.P.,Murakami, S.
Crystal structures of multidrug efflux transporters from Burkholderia pseudomallei suggest details of transport mechanism.
Proc.Natl.Acad.Sci.USA, 120:e2215072120-e2215072120, 2023

PubMed Abstract: BpeB and BpeF are multidrug efflux transporters from 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 , 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.

PubMed: 37428905
DOI: 10.1073/pnas.2215072120

Experimental method

X-RAY DIFFRACTION (3 Å)