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› 9fz5

Electron Microscopy
3.57Å resolution

Cryo-EM structure of LptDE-YedD complex from Escherichia Coli

Released:
DOI: 10.2210/pdb9fz5/pdb
PDB entry 9fz5 coloured by chain, front view.
PDB entry 9fz5 coloured by chain, side view.
PDB entry 9fz5 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Optimal functioning of the Lpt bridge depends on a ternary complex between the lipocalin YedD and the LptDE translocon.
Gennaris A, Nguyen VS, Thouvenel L, Csoma N, Vertommen D, Iorga BI, Remaut H, Collet JF
Cell Rep 44 115446 (2025)
PMID: 40127101
Related structures: EMD-50893

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-291642 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
LPS-assembly protein LptD Chain: A
Molecule details ›
Chain: A
Length: 759 amino acids
Theoretical weight: 87.08 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P31554 (Residues: 26-784; Coverage: 100%)
Gene names: JW0053, b0054, imp, lptD, ostA, yabG
Sequence domains:
LPS-assembly lipoprotein LptE Chain: B
Molecule details ›
Chain: B
Length: 149 amino acids
Theoretical weight: 16.73 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ADC1 (Residues: 20-167; Coverage: 85%)
Gene names: JW0636, b0641, lptE, rlpB
Sequence domains: Lipopolysaccharide-assembly
Uncharacterized lipoprotein YedD Chain: C

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.57Å
Relevant EMDB volumes: EMD-50893
Expression system: Escherichia coli

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