› 3sqv

X-ray diffraction
3.3Å resolution

Crystal Structure of E. coli O157:H7 E3 ubiquitin ligase, NleL, with a human E2, UbcH7

Released:
DOI: 10.2210/pdb3sqv/pdb
PDB entry 3sqv coloured by chain, front view.
PDB entry 3sqv coloured by chain, side view.
PDB entry 3sqv coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions.
Lin DY, Diao J, Chen J
Proc Natl Acad Sci U S A 109 1925-30 (2012)
PMID: 22308380

Function and Biology Details

Reactions catalysed: 
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-101894 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SopA Chains: A, B
Molecule details ›
Chains: A, B
Length: 616 amino acids
Theoretical weight: 69.7 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3JDV8 (Residues: 170-782; Coverage: 78%)
Gene names: ECs_1560, espX7
Sequence domains:
Structure domains:
Ubiquitin-conjugating enzyme E2 L3 Chains: C, D
Molecule details ›
Chains: C, D
Length: 156 amino acids
Theoretical weight: 18.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P68036 (Residues: 1-154; Coverage: 100%)
Gene names: UBCE7, UBCH7, UBE2L3
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

2 bound ligands:
Ligand SO4 9 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 302.313Å b: 72.012Å c: 125.669Å
α: 90° β: 109.22° γ: 90°
R-values:
R R work R free
0.268 0.266 0.298
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

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

4 mentions without citation

Current Understanding of the Structure and Function of Pentapeptide Repeat Proteins.
Zhang et al. (2021)
3 more