› 3sb9

X-ray diffraction
2.45Å resolution

Cu-mediated Dimer of T4 Lysozyme R76H/R80H by Synthetic Symmetrization

Released:
DOI: 10.2210/pdb3sb9/pdb
PDB entry 3sb9 coloured by chain, front view.
PDB entry 3sb9 coloured by chain, side view.
PDB entry 3sb9 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
An approach to crystallizing proteins by metal-mediated synthetic symmetrization.
Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO
Protein Sci 20 1876-90 (2011)
PMID: 21898649

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.57 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-162; Coverage: 99%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
Ligand FMT 2 x FMT
Ligand CU 1 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P41
Unit cell:
a: 79.114Å b: 79.114Å c: 87.367Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.239
Expression system: Escherichia coli

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Citations

9 review citations

The design of symmetric protein nanomaterials comes of age in theory and practice.
Yeates et al. (2016)
8 more