6HS3

Crystal structure of an ABC transporter related protein from Burkholderia pseudomallei

Replaces:  6FLX

Summary for 6HS3

• Entry DOI: 10.2210/pdb6hs3/pdb
• Descriptor: ABC transporter family protein, CHLORIDE ION (3 entities in total)
• Functional Keywords: abc transporter, burkholderia pseudomallei, transport protein, atp-binding protein, cytosolic protein
• Biological source: Burkholderia pseudomallei (Pseudomonas pseudomallei)
• Total number of polymer chains: 2
• Total formula weight: 56776.17

Authors

Pankov, G.,Hunter, W.N.,Dawson, A. (deposition date: 2018-09-28, release date: 2018-11-07, Last modification date: 2024-01-24)

Primary citation

Pankov, G.,Dawson, A.,Hunter, W.N.
The structure of lipopolysaccharide transport protein B (LptB) from Burkholderia pseudomallei.
Acta Crystallogr.,Sect.F, 75:227-232, 2019

PubMed 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 LptBFG 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.

PubMed: 30950822
DOI: 10.1107/S2053230X19001778

Experimental method

X-RAY DIFFRACTION (2.4 Å)