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› 6lbk

X-ray diffraction
2.5Å resolution

Structure of rat GLD-2 (Terminal nucleotidyltransferase 2, TENT2)

Released:
DOI: 10.2210/pdb6lbk/pdb
Model geometry
Fit model/data
PDB entry 6lbk coloured by chain, front view.
PDB entry 6lbk coloured by chain, side view.
PDB entry 6lbk coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structures of mammalian GLD-2 proteins reveal molecular basis of their functional diversity in mRNA and microRNA processing.
Ma XY, Zhang H, Feng JX, Hu JL, Yu B, Luo L, Cao YL, Liao S, Wang J, Gao S
OpenAccess logo Nucleic Acids Res 48 8782-8795 (2020)
PMID: 32633758

Function and Biology Details

Reaction catalysed: 
RNA(n) + ATP = RNA(n)-3'-adenine ribonucleotide + diphosphate.
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-178344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(A) RNA polymerase GLD2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 380 amino acids
Theoretical weight: 43.82 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5U315 (Residues: 131-484; Coverage: 73%)
Gene names: Gld2, Palp4, Tent2
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 79.96Å b: 40.72Å c: 105Å
α: 90° β: 100.204° γ: 90°
R-values:
R R work R free
0.207 0.205 0.243
Expression system: Escherichia coli

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Citations

2 citation in other articles

Gld2 activity and RNA specificity is dynamically regulated by phosphorylation and interaction with QKI-7.
Chung et al. (2021)
1 more

1 mention without citation

Structures of mammalian GLD-2 proteins reveal molecular basis of their functional diversity in mRNA and microRNA processing.
Ma et al. (2020)