8HPN

LpqY-SugABC in state 3

8HPN の概要

• エントリーDOI: 10.2210/pdb8hpn/pdb
• EMDBエントリー: 34934
• 分子名称: ABC sugar transporter, permease component, ABC transporter, permease protein SugB, ABC transporter, ATP-binding protein SugC, ... (6 entities in total)
• 機能のキーワード: trehalose, abc transporter, tuberculosis, transport protein
• 由来する生物種: Mycolicibacterium smegmatis MC2 155; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 201523.69

構造登録者

Liang, J.,Yang, X.,Zhang, B.,Rao, Z.,Liu, F. (登録日: 2022-12-12, 公開日: 2023-09-06, 最終更新日: 2023-10-18)

主引用文献

Liang, J.,Yang, X.,Hu, T.,Gao, Y.,Yang, Q.,Yang, H.,Peng, W.,Zhou, X.,Guddat, L.W.,Zhang, B.,Rao, Z.,Liu, F.
Structural insights into trehalose capture and translocation by mycobacterial LpqY-SugABC.
Structure, 31:1158-1165.e3, 2023

PubMed Abstract: The human pathogen, Mycobacterium tuberculosis (Mtb) relies heavily on trehalose for both survival and pathogenicity. The type I ATP-binding cassette (ABC) transporter LpqY-SugABC is the only trehalose import pathway in Mtb. Conformational dynamics of ABC transporters is an important feature to explain how they operate, but experimental structures are determined in a static environment. Therefore, a detailed transport mechanism cannot be elucidated because there is a lack of intermediate structures. Here, we used single-particle cryo-electron microscopy (cryo-EM) to determine the structure of the Mycobacterium smegmatis (M. smegmatis) trehalose-specific importer LpqY-SugABC complex in five different conformations. These structures have been classified and reconstructed from a single cryo-EM dataset. This study allows a comprehensive understanding of the trehalose recycling mechanism in Mycobacteria and also demonstrates the potential of single-particle cryo-EM to explore the dynamic structures of other ABC transporters and molecular machines.

PubMed: 37619560
DOI: 10.1016/j.str.2023.07.014

実験手法

ELECTRON MICROSCOPY (4.55 Å)