6hs3 | pdb_00006hs3
Crystal structure of an ABC transporter related protein from Burkholderia pseudomallei
Structural highlights
FunctionPublication Abstract from PubMedThe 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. The structure of lipopolysaccharide transport protein B (LptB) from Burkholderia pseudomallei.,Pankov G, Dawson A, Hunter WN Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):227-232. doi:, 10.1107/S2053230X19001778. Epub 2019 Mar 13. PMID:30950822[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
