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The structure of lipopolysaccharide transport protein B (LptB) from Burkholderia pseudomallei
Author(s) -
Pankov Genady,
Dawson Alice,
Hunter William N.
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19001778
Subject(s) - lipid a , bacterial outer membrane , lipopolysaccharide , intracellular , gram negative bacteria , chemistry , lipid bilayer , burkholderia pseudomallei , bacteria , membrane , biochemistry , biology , microbiology and biotechnology , biophysics , escherichia coli , gene , genetics , endocrinology
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 2 FG 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.