› 3sba

X-ray diffraction
2.75Å resolution

Zn-mediated Hexamer of T4 Lysozyme R76H/R80H by Synthetic Symmetrization

Released:
DOI: 10.2210/pdb3sba/pdb
PDB entry 3sba coloured by chain, front view.
PDB entry 3sba coloured by chain, side view.
PDB entry 3sba 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 hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133032 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
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 ZN 3 x ZN
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 55.47Å b: 137.78Å c: 146.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.278
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

3 mentions without citation

Editorial for the Special Issue of Biophysical Reviews focused on the Biophysical Society of Japan with select scientific content from the 57th BSJ annual meeting, Miyazaki, Japan.
Komatsuzaki et al. (2020)
2 more