7WLV

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

7WLV の概要

• エントリーDOI: 10.2210/pdb7wlv/pdb
• 関連するPDBエントリー: 7WLS
• 分子名称: Efflux pump membrane transporter, DODECYL-BETA-D-MALTOSIDE (3 entities in total)
• 機能のキーワード: membrane protein, transport protein
• 由来する生物種: Burkholderia pseudomallei K96243
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 695106.93

構造登録者

Kato, T.,Hung, L.-W.,Yamashita, E.,Okada, U.,Terwilliger, T.C.,Murakami, S. (登録日: 2022-01-13, 公開日: 2023-07-19, 最終更新日: 2023-11-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3 Å)