6mjp | pdb_00006mjp

LptB(E163Q)FGC from Vibrio cholerae

spinqualitylabelsall models 6mjp, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mjp is a 5 chain structure with sequence from "bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AE3, CA, CL, GOL, JU7, LMT, MA4, PEG, PG4 Gene: lptB ("Bacillo virgola del Koch" Trevisan 1884), lptC ("Bacillo virgola del Koch" Trevisan 1884), lptF ("Bacillo virgola del Koch" Trevisan 1884), lptG ("Bacillo virgola del Koch" Trevisan 1884) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A085S5D1_VIBCL] Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.[HAMAP-Rule:MF_01915] Required for the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.[PIRNR:PIRNR028513] Publication Abstract from PubMed Gram-negative bacteria are surrounded by an inner cytoplasmic membrane and by an outer membrane, which serves as a protective barrier to limit entry of many antibiotics. The distinctive properties of the outer membrane are due to the presence of lipopolysaccharide(1). This large glycolipid, which contains numerous sugars, is made in the cytoplasm; a complex of proteins forms a membrane-to-membrane bridge that mediates transport of lipopolysaccharide from the inner membrane to the cell surface(1). The inner-membrane components of the protein bridge comprise an ATP-binding cassette transporter that powers transport, but how this transporter ensures unidirectional lipopolysaccharide movement across the bridge to the outer membrane is unknown(2). Here we describe two crystal structures of a five-component inner-membrane complex that contains all the proteins required to extract lipopolysaccharide from the membrane and pass it to the protein bridge. Analysis of these structures, combined with biochemical and genetic experiments, identifies the path of lipopolysaccharide entry into the cavity of the transporter and up to the bridge. We also identify a protein gate that must open to allow movement of substrate from the cavity onto the bridge. Lipopolysaccharide entry into the cavity is ATP-independent, but ATP is required for lipopolysaccharide movement past the gate and onto the bridge. Our findings explain how the inner-membrane transport complex controls efficient unidirectional transport of lipopolysaccharide against its concentration gradient. Structural basis of unidirectional export of lipopolysaccharide to the cell surface.,Owens TW, Taylor RJ, Pahil KS, Bertani BR, Ruiz N, Kruse AC, Kahne D Nature. 2019 Mar;567(7749):550-553. doi: 10.1038/s41586-019-1039-0. Epub 2019 Mar, 20. PMID:30894747 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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