› 4nku

X-ray diffraction
1.94Å resolution

Structure of Cid1 in complex with its short product ApU

Released:
DOI: 10.2210/pdb4nku/pdb
PDB entry 4nku coloured by chain, front view.
PDB entry 4nku coloured by chain, side view.
PDB entry 4nku coloured by chain, top view.
Source organism: Schizosaccharomyces pombe
Primary publication:
A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure.
Munoz-Tello P, Gabus C, Thore S
Nucleic Acids Res 42 3372-80 (2014)
PMID: 24322298

Function and Biology Details

Reactions catalysed: 
ATP + RNA(n) = diphosphate + RNA(n+1)
UTP + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126920 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Terminal uridylyltransferase cid1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 341 amino acids
Theoretical weight: 38.98 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O13833 (Residues: 40-377; Coverage: 84%)
Gene names: SPAC19D5.03, cid1
Sequence domains:
Structure domains:
5'-R(*AP*U)-3' Chains: D, H
Molecule details ›
Chains: D, H
Length: 2 nucleotides
Theoretical weight: 590 Da
Source organism: Schizosaccharomyces pombe
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand BR 3 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 54.02Å b: 77.09Å c: 81.83Å
α: 90° β: 90.71° γ: 90°
R-values:
R R work R free
0.181 0.179 0.226
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

2 review citations

Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases.
Liudkovska et al. (2021)
1 more

6 mentions without citation

Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.
Faehnle et al. (2017)
5 more