› 2kkx

Solution NMR

Solution Structure of C-terminal domain of reduced NleG2-3 (residues 90-191) from Pathogenic E. coli O157:H7. Northeast Structural Genomics Consortium and Midwest Center for Structural Genomics target ET109A

Released:
DOI: 10.2210/pdb2kkx/pdb
PDB entry 2kkx coloured by chain, ensemble of 20 models, front view.
PDB entry 2kkx coloured by chain, ensemble of 20 models, side view.
PDB entry 2kkx coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
NleG Type 3 effectors from enterohaemorrhagic Escherichia coli are U-Box E3 ubiquitin ligases.
Wu B, Skarina T, Yee A, Jobin MC, Dileo R, Semesi A, Fares C, Lemak A, Coombes BK, Arrowsmith CH, Singer AU, Savchenko A
PLoS Pathog 6 e1000960 (2010)
PMID: 20585566

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
T3SS secreted effector NleG Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.29 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8X509 (Residues: 90-191; Coverage: 53%)
Gene names: ECs_2156, nleG2-3
Sequence domains: Effector protein NleG
Structure domains: Effector protein NleG

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Ubiquitin Ligases: Structure, Function, and Regulation.
Zheng et al. (2017)
21 more

9 mentions without citation

NleG Type 3 effectors from enterohaemorrhagic Escherichia coli are U-Box E3 ubiquitin ligases.
Wu et al. (2010)
8 more