› 1myl

X-ray diffraction
2.4Å resolution

SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY

Released:
DOI: 10.2210/pdb1myl/pdb
PDB entry 1myl coloured by chain, front view.
PDB entry 1myl coloured by chain, side view.
PDB entry 1myl coloured by chain, top view.
Source organism: Salmonella virus P22
Primary publication:
Are buried salt bridges important for protein stability and conformational specificity?
Waldburger CD, Schildbach JF, Sauer RT
Nat Struct Biol 2 122-8 (1995)
PMID: 7749916

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136487 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcriptional repressor arc Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 53 amino acids
Theoretical weight: 6.2 KDa
Source organism: Salmonella virus P22
Expression system: Escherichia coli
UniProt:
  • Canonical: P03050 (Residues: 1-53; Coverage: 100%)
Gene name: arc
Sequence domains: Arc-like DNA binding domain
Structure domains: Met repressor-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 29.6Å b: 117.1Å c: 49.7Å
α: 90° β: 98.6° γ: 90°
R-values:
R R work R free
0.209 0.209 0.293
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Membrane protein folding and stability: physical principles.
White et al. (1999)
21 more

2 mentions without citation

Mechanisms of toxin inhibition and transcriptional repression by Escherichia coli DinJ-YafQ.
Ruangprasert et al. (2014)
1 more