› 2rpi

Solution NMR

The NMR structure of the submillisecond folding intermediate of the Thermus thermophilus ribonuclease H

Released:
DOI: 10.2210/pdb2rpi/pdb
PDB entry 2rpi coloured by chain, ensemble of 10 models, front view.
PDB entry 2rpi coloured by chain, ensemble of 10 models, side view.
PDB entry 2rpi coloured by chain, ensemble of 10 models, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H.
Zhou Z, Feng H, Ghirlando R, Bai Y
J Mol Biol 384 531-9 (2008)
PMID: 18848567

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151372 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease H Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.88 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: P29253 (Residues: 1-127; Coverage: 64%)
Gene names: TTHA1556, 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
Refinement method: DGSA-distance geometry simulated annealing, torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The folding of single domain proteins--have we reached a consensus?
Sosnick et al. (2011)
3 more

1 mention without citation

The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H.
Zhou et al. (2008)