+Open data
-Basic information
Entry | Database: PDB / ID: 6mhu | ||||||
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Title | Nucleotide-free Cryo-EM Structure of E.coli LptB2FG Transporter | ||||||
Components |
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Keywords | TRANSPORT PROTEIN/Hydrolase / ABC transporter / lipopolysaccharide / LPS / nanodisc / TRANSPORT PROTEIN-Hydrolase complex | ||||||
Function / homology | Function and homology information Translocases; Catalysing the translocation of carbohydrates and their derivatives; Linked to the hydrolysis of a nucleoside triphosphate / transporter complex / lipopolysaccharide transport / Gram-negative-bacterium-type cell outer membrane assembly / ATP-binding cassette (ABC) transporter complex / transmembrane transport / ATP hydrolysis activity / ATP binding / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å | ||||||
Authors | Orlando, B.J. / Li, Y. / Liao, M. | ||||||
Funding support | United States, 1items
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Citation | Journal: Nature / Year: 2019 Title: Structural basis of lipopolysaccharide extraction by the LptBFGC complex. Authors: Yanyan Li / Benjamin J Orlando / Maofu Liao / Abstract: In Gram-negative bacteria, lipopolysaccharide is essential for outer membrane formation and antibiotic resistance. The seven lipopolysaccharide transport (Lpt) proteins A-G move lipopolysaccharide ...In Gram-negative bacteria, lipopolysaccharide is essential for outer membrane formation and antibiotic resistance. The seven lipopolysaccharide transport (Lpt) proteins A-G move lipopolysaccharide from the inner to the outer membrane. The ATP-binding cassette transporter LptBFG, which tightly associates with LptC, extracts lipopolysaccharide out of the inner membrane. The mechanism of the LptBFG-LptC complex (LptBFGC) and the role of LptC in lipopolysaccharide transport are poorly understood. Here we characterize the structures of LptBFG and LptBFGC in nucleotide-free and vanadate-trapped states, using single-particle cryo-electron microscopy. These structures resolve the bound lipopolysaccharide, reveal transporter-lipopolysaccharide interactions with side-chain details and uncover how the capture and extrusion of lipopolysaccharide are coupled to conformational rearrangements of LptBFGC. LptC inserts its transmembrane helix between the two transmembrane domains of LptBFG, which represents a previously unknown regulatory mechanism for ATP-binding cassette transporters. Our results suggest a role for LptC in achieving efficient lipopolysaccharide transport, by coordinating the action of LptBFG in the inner membrane and Lpt protein interactions in the periplasm. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6mhu.cif.gz | 210.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6mhu.ent.gz | 162.9 KB | Display | PDB format |
PDBx/mmJSON format | 6mhu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6mhu_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 6mhu_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6mhu_validation.xml.gz | 41.3 KB | Display | |
Data in CIF | 6mhu_validation.cif.gz | 61.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mh/6mhu ftp://data.pdbj.org/pub/pdb/validation_reports/mh/6mhu | HTTPS FTP |
-Related structure data
Related structure data | 9118MC 9124C 9125C 9126C 9128C 9129C 9130C 6mhzC 6mi7C 6mi8C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 40393.473 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (strain K12) (bacteria) Strain: K12 / Gene: lptF, yjgP, b4261, JW4218 / Production host: Escherichia coli (E. coli) / References: UniProt: P0AF98 | ||
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#2: Protein | Mass: 39651.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (strain K12) (bacteria) Strain: K12 / Gene: lptG, yjgQ, b4262, JW5760 / Production host: Escherichia coli (E. coli) / References: UniProt: P0ADC6 | ||
#3: Protein | Mass: 28131.088 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (strain K12) (bacteria) Strain: K12 / Gene: lptB, yhbG, b3201, JW3168 / Production host: Escherichia coli (E. coli) References: UniProt: P0A9V1, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances #4: Chemical | ChemComp-JSG / ( | |