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Structural and functional insights into the lipopolysaccharide ABC transporter LptB2FG

DOI: 10.1038/s41467-017-00273-5 DOI Help

Authors: Haohao Dong (Sichuan University and Collaborative Innovation Center of Biotherapy) , Zhengyu Zhang (University of East Anglia) , Xiaodi Tang (University of East Anglia; University of Oxford) , Neil G. Paterson (Diamond Light Source) , Changjiang Dong (University of East Anglia)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: August 2017
Diamond Proposal Number(s): 9475

Open Access Open Access

Abstract: The cell surface of most Gram-negative bacteria contains lipopolysaccharide that is essential for their viability and drug resistance. A 134-kDa protein complex LptB2FG is unique among ATP-binding cassette transporters because it extracts lipopolysaccharide from the external leaflet of the inner membrane and propels it along a filament that extends across the periplasm to directly deliver lipopolysaccharide into the external leaflet of the outer membrane. Here we report the crystal structure of the lipopolysaccharide transporter LptB2FG from Klebsiella pneumoniae, in which both LptF and LptG are composed of a β-jellyroll-like periplasmic domain and six α-helical segments in the transmembrane domain. LptF and LptG form a central cavity containing highly conserved hydrophobic residues. Structural and functional studies suggest that LptB2FG uses an alternating lateral access mechanism to extract lipopolysaccharide and traffic it along the hydrophobic cavity toward the transporter’s periplasmic domains.

Journal Keywords: Bacteriology; Membrane structure and assembly; X-ray crystallography

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I03-Macromolecular Crystallography

Added On: 10/08/2017 09:41


Discipline Tags:

Pathogens Antibiotic Resistance Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)