› 1hzc

X-ray diffraction
1.32Å resolution

BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY

Released:
DOI: 10.2210/pdb1hzc/pdb
PDB entry 1hzc coloured by chain, front view.
PDB entry 1hzc coloured by chain, side view.
PDB entry 1hzc coloured by chain, top view.
Source organism: [Bacillus] caldolyticus
Primary publication:
Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability.
Delbrück H, Mueller U, Perl D, Schmid FX, Heinemann U
J Mol Biol 313 359-69 (2001)
PMID: 11800562

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cold shock protein CspB Chains: A, B
Molecule details ›
Chains: A, B
Length: 66 amino acids
Theoretical weight: 7.27 KDa
Source organism: [Bacillus] caldolyticus
Expression system: Escherichia coli
UniProt:
  • Canonical: P41016 (Residues: 1-66; Coverage: 100%)
Gene name: cspB
Sequence domains: 'Cold-shock' DNA-binding domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: I41
Unit cell:
a: 76.864Å b: 76.864Å c: 48.024Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.139 0.181
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Selection of mutations for increased protein stability.
van den Burg et al. (2002)
3 more