› 2i5m

X-ray diffraction
2.3Å resolution

Crystal structure of Bacillus subtilis cold shock protein CspB variant A46K S48R

Released:
DOI: 10.2210/pdb2i5m/pdb
PDB entry 2i5m coloured by chain, front view.
PDB entry 2i5m coloured by chain, side view.
PDB entry 2i5m coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Optimized variants of the cold shock protein from in vitro selection: structural basis of their high thermostability.
Max KE, Wunderlich M, Roske Y, Schmid FX, Heinemann U
J Mol Biol 369 1087-97 (2007)
PMID: 17481655

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cold shock protein CspB Chain: X
Molecule details ›
Chain: X
Length: 67 amino acids
Theoretical weight: 7.5 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P32081 (Residues: 1-67; Coverage: 100%)
Gene names: BSU09100, cspA, cspB
Sequence domains: 'Cold-shock' DNA-binding domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P3221
Unit cell:
a: 58.627Å b: 58.627Å c: 46.798Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.204 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Cold-Shock Domains-Abundance, Structure, Properties, and Nucleic-Acid Binding.
Heinemann et al. (2021)
1 more