8TSS

Open, inward-facing MsbA structure (OIF3)

8TSS の概要

• エントリーDOI: 10.2210/pdb8tss/pdb
• EMDBエントリー: 41596 41597 41598 41599 41600
• 分子名称: ATP-binding transport protein MsbA (1 entity in total)
• 機能のキーワード: abc transporter, transport protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 129086.95

構造登録者

Yang, B.,Zhang, T.,Lyu, J.,Laganowsky, A.D.,Zhao, M. (登録日: 2023-08-11, 公開日: 2024-06-19, 最終更新日: 2025-05-21)

主引用文献

Zhang, T.,Lyu, J.,Yang, B.,Yun, S.D.,Scott, E.,Zhao, M.,Laganowsky, A.
Native mass spectrometry and structural studies reveal modulation of MsbA-nucleotide interactions by lipids.
Nat Commun, 15:5946-5946, 2024

PubMed Abstract: The ATP-binding cassette (ABC) transporter, MsbA, plays a pivotal role in lipopolysaccharide (LPS) biogenesis by facilitating the transport of the LPS precursor lipooligosaccharide (LOS) from the cytoplasmic to the periplasmic leaflet of the inner membrane. Despite multiple studies shedding light on MsbA, the role of lipids in modulating MsbA-nucleotide interactions remains poorly understood. Here we use native mass spectrometry (MS) to investigate and resolve nucleotide and lipid binding to MsbA, demonstrating that the transporter has a higher affinity for adenosine 5'-diphosphate (ADP). Moreover, native MS shows the LPS-precursor 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo)-lipid A (KDL) can tune the selectivity of MsbA for adenosine 5'-triphosphate (ATP) over ADP. Guided by these studies, four open, inward-facing structures of MsbA are determined that vary in their openness. We also report a 2.7 Å-resolution structure of MsbA in an open, outward-facing conformation that is not only bound to KDL at the exterior site, but with the nucleotide binding domains (NBDs) adopting a distinct nucleotide-free structure. The results obtained from this study offer valuable insight and snapshots of MsbA during the transport cycle.

PubMed: 39009687
DOI: 10.1038/s41467-024-50350-9

実験手法

ELECTRON MICROSCOPY (3.7 Å)