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


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.

SUBMITTER: Pankov G 

PROVIDER: S-EPMC6450526 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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

Pankov Genady G   Dawson Alice A   Hunter William N WN  

Acta crystallographica. Section F, Structural biology communications 20190313 Pt 4


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 LptB<sub>2</sub>FG protein complex extracts lip  ...[more]

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