› 1c9o

X-ray diffraction
1.17Å resolution

CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP

Released:
DOI: 10.2210/pdb1c9o/pdb
PDB entry 1c9o coloured by chain, front view.
PDB entry 1c9o coloured by chain, side view.
PDB entry 1c9o coloured by chain, top view.
Source organism: [Bacillus] caldolyticus
Primary publication:
Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein.
Mueller U, Perl D, Schmid FX, Heinemann U
J Mol Biol 297 975-88 (2000)
PMID: 10736231

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: 7.34 KDa
Source organism: [Bacillus] caldolyticus
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

2 bound ligands:
Ligand NA 2 x NA
Ligand TRS 3 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: I41
Unit cell:
a: 76.995Å b: 76.995Å c: 47.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 0.124 0.179

Quick links

Citations

9 review citations

From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding.
Shea et al. (2001)
8 more

29 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
28 more