› 1lwk

X-ray diffraction
2.1Å resolution

Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability

Released:
DOI: 10.2210/pdb1lwk/pdb
PDB entry 1lwk coloured by chain, front view.
PDB entry 1lwk coloured by chain, side view.
PDB entry 1lwk coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Gassner NC, Baase WA, Mooers BH, Busam RD, Weaver LH, Lindstrom JD, Quillin ML, Matthews BW
Biophys Chem 100 325-40 (2003)
PMID: 12646375

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 19.54 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
Ligand CL 2 x CL
Ligand HED 1 x HED
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P3221
Unit cell:
a: 60.332Å b: 60.332Å c: 91.367Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.217 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Isosteric replacement of sulfur with other chalcogens in peptides and proteins.
Moroder L. (2005)
1 more

1 mention without citation

TSpred: a web server for the rational design of temperature-sensitive mutants.
Tan et al. (2014)