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› 4k25

X-ray diffraction
2.88Å resolution

Crystal Structure of yeast Qri7 homodimer

Released:
DOI: 10.2210/pdb4k25/pdb
Model geometry
Fit model/data
PDB entry 4k25 coloured by chain, front view.
PDB entry 4k25 coloured by chain, side view.
PDB entry 4k25 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system.
Wan LC, Mao DY, Neculai D, Strecker J, Chiovitti D, Kurinov I, Poda G, Thevakumaran N, Yuan F, Szilard RK, Lissina E, Nislow C, Caudy AA, Durocher D, Sicheri F
OpenAccess logo Nucleic Acids Res 41 6332-46 (2013)
PMID: 23620299

Function and Biology Details

Reaction catalysed: 
L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-threonylcarbamoyladenosine(37) in tRNA + AMP + H(+).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154954 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 383 amino acids
Theoretical weight: 42.99 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P43122 (Residues: 30-407; Coverage: 93%)
Gene names: D2366, QRI7, YDL104C
Sequence domains: tRNA N6-adenosine threonylcarbamoyltransferase
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand CA 1 x CA
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21212
Unit cell:
a: 64.597Å b: 130.983Å c: 47.866Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.24 0.295
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Naturally occurring modified ribonucleosides.
McCown et al. (2020)
10 more

4 mentions without citation

The structural and functional workings of KEOPS.
Beenstock et al. (2021)
3 more