› 2e4l

X-ray diffraction
2Å resolution

Thermodynamic and Structural Analysis of Thermolabile RNase HI from Shewanella oneidensis MR-1

Released:
DOI: 10.2210/pdb2e4l/pdb
PDB entry 2e4l coloured by chain, front view.
PDB entry 2e4l coloured by chain, side view.
PDB entry 2e4l coloured by chain, top view.
Source organism: Shewanella oneidensis MR-1
Primary publication:
Structural, thermodynamic, and mutational analyses of a psychrotrophic RNase HI.
Tadokoro T, You DJ, Abe Y, Chon H, Matsumura H, Koga Y, Takano K, Kanaya S
Biochemistry 46 7460-8 (2007)
PMID: 17536836

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HI Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.81 KDa
Source organism: Shewanella oneidensis MR-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EE30 (Residues: 1-158; Coverage: 100%)
Gene names: SO_2560, rnhA
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P422
Unit cell:
a: 77.128Å b: 77.128Å c: 76.661Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.219
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes.
Tadokoro et al. (2009)
5 other articles

6 mentions without citation

Thermal adaptation of conformational dynamics in ribonuclease H.
Stafford et al. (2013)
5 more