4P33

Crystal structure of E. coli LptB-E163Q in complex with ATP-sodium

4P33 の概要

• エントリーDOI: 10.2210/pdb4p33/pdb
• 関連するPDBエントリー: 4P31 4P32
• 分子名称: Lipopolysaccharide export system ATP-binding protein LptB, SODIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: abc transporter, nucleotide-binding domain, atpase, atp binding, hydrolase
• 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: 57400.36

構造登録者

Sherman, D.J.,Lazarus, M.B.,Murphy, L.,Liu, C.,Walker, S.,Ruiz, N.,Kahne, D. (登録日: 2014-03-05, 公開日: 2014-03-26, 最終更新日: 2023-09-27)

主引用文献

Sherman, D.J.,Lazarus, M.B.,Murphy, L.,Liu, C.,Walker, S.,Ruiz, N.,Kahne, D.
Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport.
Proc.Natl.Acad.Sci.USA, 111:4982-4987, 2014

PubMed Abstract: The cell surface of Gram-negative bacteria contains lipopolysaccharides (LPS), which provide a barrier against the entry of many antibiotics. LPS assembly involves a multiprotein LPS transport (Lpt) complex that spans from the cytoplasm to the outer membrane. In this complex, an unusual ATP-binding cassette transporter is thought to power the extraction of LPS from the outer leaflet of the cytoplasmic membrane and its transport across the cell envelope. We introduce changes into the nucleotide-binding domain, LptB, that inactivate transporter function in vivo. We characterize these residues using biochemical experiments combined with high-resolution crystal structures of LptB pre- and post-ATP hydrolysis and suggest a role for an active site residue in phosphate exit. We also identify a conserved residue that is not required for ATPase activity but is essential for interaction with the transmembrane components. Our studies establish the essentiality of ATP hydrolysis by LptB to power LPS transport in cells and suggest strategies to inhibit transporter function away from the LptB active site.

PubMed: 24639492
DOI: 10.1073/pnas.1323516111

実験手法

X-RAY DIFFRACTION (1.65 Å)