8QKK
Cryo-EM structure of MmpL3 from Mycobacterium smegmatis reconstituted into peptidiscs
8QKK の概要
| エントリーDOI | 10.2210/pdb8qkk/pdb |
| EMDBエントリー | 18464 |
| 分子名称 | Trehalose monomycolate exporter MmpL3 (1 entity in total) |
| 機能のキーワード | mycobacterium, trehalose monomycolate, tmm, peptidisc, mmpl3, membrane protein |
| 由来する生物種 | Mycolicibacterium smegmatis MC2 155 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 85465.34 |
| 構造登録者 | Couston, J.,Guo, Z.,Wang, K.,Gourdon, P.E.,Blaise, M. (登録日: 2023-09-15, 公開日: 2023-11-15, 最終更新日: 2023-12-13) |
| 主引用文献 | Couston, J.,Guo, Z.,Wang, K.,Gourdon, P.,Blaise, M. Cryo-EM structure of the trehalose monomycolate transporter, MmpL3, reconstituted into peptidiscs. Curr Res Struct Biol, 6:100109-100109, 2023 Cited by PubMed Abstract: Mycobacteria have an atypical thick and waxy cell wall. One of the major building blocks of such mycomembrane is trehalose monomycolate (TMM). TMM is a mycolic acid ester of trehalose that possesses long acyl chains with up to 90 carbon atoms. TMM represents an essential component of mycobacteria and is synthesized in the cytoplasm, and then flipped over the plasma membrane by a specific transporter known as MmpL3. Over the last decade, MmpL3 has emerged as an attractive drug target to combat mycobacterial infections. Recent three-dimensional structures of MmpL3 determined by X-ray crystallography and cryo-EM have increased our understanding of the TMM transport, and the mode of action of inhibiting compounds. These structures were obtained in the presence of detergent and/or in a lipidic environment. In this study, we demonstrate the possibility of obtaining a high-quality cryo-EM structure of MmpL3 without any presence of detergent through the reconstitution of the protein into peptidiscs. The structure was determined at an overall resolution of 3.2 Å and demonstrates that the overall structure of MmpL3 is preserved as compared to previous structures. Further, the study identified a new structural arrangement of the linker that fuses the two subdomains of the transmembrane domain, suggesting the feature may serve a role in the transport process. PubMed: 38034087DOI: 10.1016/j.crstbi.2023.100109 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.23 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






