5IV9

The LPS Transporter LptDE from Klebsiella pneumoniae, full-length

5IV9 の概要

• エントリーDOI: 10.2210/pdb5iv9/pdb
• 関連するPDBエントリー: 5IV8 5IVA
• 分子名称: LPS-assembly protein LptD, LPS-assembly lipoprotein LptE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total)
• 機能のキーワード: lptd, lpte, lipopolysaccharide, transporter, transport protein
• 由来する生物種: Klebsiella pneumoniae; 詳細
• 細胞内の位置: Cell outer membrane : C4T9I0; Cell outer membrane ; Lipid-anchor : A0A0J4W1Y0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105997.67

構造登録者

Botos, I.,McCarthy, J.G.,Buchanan, S.K. (登録日: 2016-03-20, 公開日: 2016-05-18, 最終更新日: 2024-10-16)

主引用文献

Botos, I.,Majdalani, N.,Mayclin, S.J.,McCarthy, J.G.,Lundquist, K.,Wojtowicz, D.,Barnard, T.J.,Gumbart, J.C.,Buchanan, S.K.
Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.
Structure, 24:965-976, 2016

PubMed Abstract: Incorporation of lipopolysaccharide (LPS) into the outer membrane of Gram-negative bacteria is essential for viability, and is accomplished by a two-protein complex called LptDE. We solved crystal structures of the core LptDE complexes from Yersinia pestis, Klebsiella pneumoniae, Pseudomonas aeruginosa, and a full-length structure of the K. pneumoniae LptDE complex. Our structures adopt the same plug and 26-strand β-barrel architecture found recently for the Shigella flexneri and Salmonella typhimurium LptDE structures, illustrating a conserved fold across the family. A comparison of the only two full-length structures, SfLptDE and our KpLptDE, reveals a 21° rotation of the LptD N-terminal domain that may impart flexibility on the trans-envelope LptCAD scaffold. Utilizing mutagenesis coupled to an in vivo functional assay and molecular dynamics simulations, we demonstrate the critical role of Pro231 and Pro246 in the function of the LptD lateral gate that allows partitioning of LPS into the outer membrane.

PubMed: 27161977
DOI: 10.1016/j.str.2016.03.026

実験手法

X-RAY DIFFRACTION (4.369 Å)