› 2lnh

Solution NMR

Enterohaemorrhagic E. coli (EHEC) exploits a tryptophan switch to hijack host F-actin assembly

Released:
DOI: 10.2210/pdb2lnh/pdb
PDB entry 2lnh coloured by chain, ensemble of 20 models, front view.
PDB entry 2lnh coloured by chain, ensemble of 20 models, side view.
PDB entry 2lnh coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly.
Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P
Structure 20 1692-703 (2012)
PMID: 22921828

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-126257 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Actin nucleation-promoting factor WASL Chain: A
Molecule details ›
Chain: A
Length: 65 amino acids
Theoretical weight: 7.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00401 (Residues: 207-270; Coverage: 13%)
Gene name: WASL
Sequence domains: P21-Rho-binding domain
Structure domains: CRIB domain
BAR/IMD domain-containing adapter protein 2-like 1 Chain: B
Molecule details ›
Chain: B
Length: 67 amino acids
Theoretical weight: 7.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UHR4 (Residues: 339-402; Coverage: 13%)
Gene names: BAIAP2L1, IRTKS
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains
Secreted effector protein EspF(U) Chain: C
Molecule details ›
Chain: C
Length: 48 amino acids
Theoretical weight: 5.3 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DJ89 (Residues: 268-314; Coverage: 14%)
Gene names: espF(U), tccP
Sequence domains: EspF protein repeat
Structure domains: TccP2/EspF(U)-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Refinement method: torsion angle dynamics, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The most important thing is the tail: multitudinous functionalities of intrinsically disordered protein termini.
Uversky VN. (2013)
4 more

1 mention without citation

Interesting Biochemistries in the Structure and Function of Bacterial Effectors.
Mak et al. (2021)