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5L75

A protein structure

Summary for 5L75
Entry DOI10.2210/pdb5l75/pdb
DescriptorLipopolysaccharide ABC transporter, ATP-binding protein LptB, FIG000988: Predicted permease, FIG000906: Predicted Permease, ... (4 entities in total)
Functional Keywordsgram-negative bacteria, transport protein
Biological sourceKlebsiella pneumoniae IS22
More
Total number of polymer chains4
Total formula weight134293.70
Authors
Dong, C.,Dong, H.,Zhang, Z.,Paterson, N.,Tang, X. (deposition date: 2016-06-01, release date: 2017-08-16, Last modification date: 2024-05-08)
Primary citationDong, H.,Zhang, Z.,Tang, X.,Paterson, N.G.,Dong, C.
Structural and functional insights into the lipopolysaccharide ABC transporter LptB2FG.
Nat Commun, 8:222-222, 2017
Cited by
PubMed Abstract: The cell surface of most Gram-negative bacteria contains lipopolysaccharide that is essential for their viability and drug resistance. A 134-kDa protein complex LptBFG is unique among ATP-binding cassette transporters because it extracts lipopolysaccharide from the external leaflet of the inner membrane and propels it along a filament that extends across the periplasm to directly deliver lipopolysaccharide into the external leaflet of the outer membrane. Here we report the crystal structure of the lipopolysaccharide transporter LptBFG from Klebsiella pneumoniae, in which both LptF and LptG are composed of a β-jellyroll-like periplasmic domain and six α-helical segments in the transmembrane domain. LptF and LptG form a central cavity containing highly conserved hydrophobic residues. Structural and functional studies suggest that LptBFG uses an alternating lateral access mechanism to extract lipopolysaccharide and traffic it along the hydrophobic cavity toward the transporter's periplasmic domains.Lipopolysaccharides (LPS) are synthesized at the periplasmic side of the inner membrane of Gram-negative bacteria and are then extracted by the LptBFG complex during the first step of LPS transport to the outer membrane. Here the authors present the LptBFG structure, which supports an alternating lateral access mechanism for LPS extraction.
PubMed: 28790314
DOI: 10.1038/s41467-017-00273-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.7 Å)
Structure validation

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数据于2024-10-30公开中

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