› 2z1j

X-ray diffraction
2.38Å resolution

Crystal structure of E.coli RNase HI surface charged mutant(Q4R/T40E/Q72H/Q76K/Q80E/T92K/Q105K/Q113R/Q115K/N143K/T145K)

Released:
DOI: 10.2210/pdb2z1j/pdb
PDB entry 2z1j coloured by chain, front view.
PDB entry 2z1j coloured by chain, side view.
PDB entry 2z1j coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Protein thermostabilization requires a fine-tuned placement of surface-charged residues.
You DJ, Fukuchi S, Nishikawa K, Koga Y, Takano K, Kanaya S
J Biochem 142 507-16 (2007)
PMID: 17761696

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-141635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HI Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.79 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7Y4 (Residues: 1-155; Coverage: 100%)
Gene names: JW0204, b0214, dasF, herA, rnh, rnhA, sdrA
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 BL38B1
Spacegroup: P3221
Unit cell:
a: 85.273Å b: 85.273Å c: 51.024Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.238
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Stabilization of enzymes in ionic liquids via modification of enzyme charge.
Nordwald et al. (2013)
3 more