› 2luq

Solution NMR

Solution structure of double-stranded RNA binding domain of S.cerevisiae RNase III (rnt1p)

Released:
DOI: 10.2210/pdb2luq/pdb
PDB entry 2luq coloured by chain, ensemble of 20 models, front view.
PDB entry 2luq coloured by chain, ensemble of 20 models, side view.
PDB entry 2luq coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Intrinsic dynamics of an extended hydrophobic core in the S. cerevisiae RNase III dsRBD contributes to recognition of specific RNA binding sites.
Hartman E, Wang Z, Zhang Q, Roy K, Chanfreau G, Feigon J
J Mol Biol 425 546-62 (2013)
PMID: 23201338

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease 3 Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 9.82 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q02555 (Residues: 366-453; Coverage: 19%)
Gene names: RNT1, YM9408.01C, YM9959.21, YMR239C
Sequence domains: Double-stranded RNA binding motif
Structure domains: Double Stranded RNA Binding Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 81%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Ribonuclease III mechanisms of double-stranded RNA cleavage.
Nicholson AW. (2014)
4 more

1 mention without citation

Intrinsic dynamics of an extended hydrophobic core in the S. cerevisiae RNase III dsRBD contributes to recognition of specific RNA binding sites.
Hartman et al. (2013)