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4N4R

Structure basis of lipopolysaccharide biogenesis

4N4R の概要
エントリーDOI10.2210/pdb4n4r/pdb
分子名称LPS-assembly protein LptD, LPS-assembly lipoprotein LptE, CACODYLATE ION, ... (5 entities in total)
機能のキーワードbeta barrel, translocase, lipopolysaccharide transport proteins, membrane protein
由来する生物種Salmonella enterica subsp. enterica serovar Typhimurium
詳細
細胞内の位置Cell outer membrane (By similarity): Q8ZRW0
Cell outer membrane; Lipid-anchor (By similarity): Q8ZQZ7
タンパク質・核酸の鎖数4
化学式量合計225816.46
構造登録者
Dong, H.,Xiang, Q.,Wang, Z.,Paterson, N.G.,He, C.,Zhang, Y.,Wang, W.,Dong, C. (登録日: 2013-10-08, 公開日: 2014-06-25, 最終更新日: 2014-07-16)
主引用文献Dong, H.,Xiang, Q.,Gu, Y.,Wang, Z.,Paterson, N.G.,Stansfeld, P.J.,He, C.,Zhang, Y.,Wang, W.,Dong, C.
Structural basis for outer membrane lipopolysaccharide insertion.
Nature, 511:52-56, 2014
Cited by
PubMed Abstract: Lipopolysaccharide (LPS) is essential for most Gram-negative bacteria and has crucial roles in protection of the bacteria from harsh environments and toxic compounds, including antibiotics. Seven LPS transport proteins (that is, LptA-LptG) form a trans-envelope protein complex responsible for the transport of LPS from the inner membrane to the outer membrane, the mechanism for which is poorly understood. Here we report the first crystal structure of the unique integral membrane LPS translocon LptD-LptE complex. LptD forms a novel 26-stranded β-barrel, which is to our knowledge the largest β-barrel reported so far. LptE adopts a roll-like structure located inside the barrel of LptD to form an unprecedented two-protein 'barrel and plug' architecture. The structure, molecular dynamics simulations and functional assays suggest that the hydrophilic O-antigen and the core oligosaccharide of the LPS may pass through the barrel and the lipid A of the LPS may be inserted into the outer leaflet of the outer membrane through a lateral opening between strands β1 and β26 of LptD. These findings not only help us to understand important aspects of bacterial outer membrane biogenesis, but also have significant potential for the development of novel drugs against multi-drug resistant pathogenic bacteria.
PubMed: 24990744
DOI: 10.1038/nature13464
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 4n4r
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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