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The structure of lipopolysaccharide transport protein B (LptB) from Burkholderia pseudomallei

DOI: 10.1107/S2053230X19001778 DOI Help

Authors: Genady Pankov (University of Dundee) , Alice Dawson (University of Dundee) , William N. Hunter (University of Dundee)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 75

State: Published (Approved)
Published: April 2019
Diamond Proposal Number(s): 14980

Abstract: The thick outer membrane (OM) of Gram-negative bacteria performs an important protective role against hostile environments, supports cell integrity, and contributes to surface adhesion and in some cases also to virulence. A major component of the OM is lipopolysaccharide (LPS), a complex glycolipid attached to a core containing fatty-acyl chains. The assembly and transport of lipid A, the membrane anchor for LPS, to the OM begins when a heteromeric LptB2FG protein complex extracts lipid A from the outer leaflet of the inner membrane. This process requires energy, and upon hydrolysis of ATP one component of the heteromeric assembly, LptB, triggers a conformational change in LptFG in support of lipid A transport. A structure of LptB from the intracellular pathogen Burkholderia pseudomallei is reported here. LptB forms a dimer that displays a relatively fixed structure irrespective of whether it is in complex with LptFG or in isolation. Highly conserved sequence and structural features are discussed that allow LptB to fuel the transport of lipid A.

Journal Keywords: ABC transporters; ATPases; lipopolysaccharide transport complex; protein–protein interactions

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography