› 3nh0

X-ray diffraction
2.3Å resolution

Crystal structure of RNase T in complex with a non-preferred ssDNA (AAC)

Released:
DOI: 10.2210/pdb3nh0/pdb
PDB entry 3nh0 coloured by chain, front view.
PDB entry 3nh0 coloured by chain, side view.
PDB entry 3nh0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation.
Hsiao YY, Yang CC, Lin CL, Lin JL, Duh Y, Yuan HS
Nat Chem Biol 7 236-43 (2011)
PMID: 21317904

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-116619 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Ribonuclease T Chains: A, B
Molecule details ›
Chains: A, B
Length: 235 amino acids
Theoretical weight: 25.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P30014 (Residues: 1-215; Coverage: 100%)
Gene names: JW1644, b1652, rnt
Sequence domains: Exonuclease
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
5'-D(*TP*TP*AP*CP*AP*AP*C)-3' Chains: C, D
Molecule details ›
Chains: C, D
Length: 7 nucleotides
Theoretical weight: 2.08 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21212
Unit cell:
a: 96.075Å b: 106.36Å c: 46.991Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.196 0.249
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Bacterial ribonucleases and their roles in RNA metabolism.
Bechhofer et al. (2019)
2 more

2 mentions without citation

Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.
Jones et al. (2022)
1 more