4Q35

Structure of a membrane protein

4Q35 の概要

• エントリーDOI: 10.2210/pdb4q35/pdb
• 分子名称: LPS-assembly protein LptD, LPS-assembly lipoprotein LptE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (6 entities in total)
• 機能のキーワード: complex, 26 beita-sheet, membrane protein, lps biogenesis
• 由来する生物種: Shigella flexneri; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115461.29

構造登録者

Huang, Y.,Qiao, S.,Luo, Q.,Zhao, Y. (登録日: 2014-04-11, 公開日: 2014-06-25, 最終更新日: 2024-10-30)

主引用文献

Qiao, S.,Luo, Q.,Zhao, Y.,Zhang, X.C.,Huang, Y.
Structural basis for lipopolysaccharide insertion in the bacterial outer membrane.
Nature, 511:108-111, 2014

PubMed Abstract: One of the fundamental properties of biological membranes is the asymmetric distribution of membrane lipids. In Gram-negative bacteria, the outer leaflet of the outer membrane is composed predominantly of lipopolysaccharides (LPS). The export of LPS requires seven essential lipopolysaccharide transport (Lpt) proteins to move LPS from the inner membrane, through the periplasm to the surface. Of the seven Lpt proteins, the LptD-LptE complex is responsible for inserting LPS into the external leaflet of the outer membrane. Here we report the crystal structure of the ∼110-kilodalton membrane protein complex LptD-LptE from Shigella flexneri at 2.4 Å resolution. The structure reveals an unprecedented two-protein plug-and-barrel architecture with LptE embedded into a 26-stranded β-barrel formed by LptD. Importantly, the secondary structures of the first two β-strands are distorted by two proline residues, weakening their interactions with neighbouring β-strands and creating a potential portal on the barrel wall that could allow lateral diffusion of LPS into the outer membrane. The crystal structure of the LptD-LptE complex opens the door to new antibiotic strategies targeting the bacterial outer membrane.

PubMed: 24990751
DOI: 10.1038/nature13484

実験手法

X-RAY DIFFRACTION (2.393 Å)