› 3w1i

X-ray diffraction
3.19Å resolution

Crystal structure of the N-terminal truncated selenocysteine synthase SelA

Released:
DOI: 10.2210/pdb3w1i/pdb
PDB entry 3w1i coloured by chain, front view.
PDB entry 3w1i coloured by chain, side view.
PDB entry 3w1i coloured by chain, top view.
Source organism: Aquifex aeolicus VF5
Primary publication:
Decameric SelA•tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation.
Itoh Y, Bröcker MJ, Sekine S, Hammond G, Suetsugu S, Söll D, Yokoyama S
Science 340 75-8 (2013)
PMID: 23559248

Function and Biology Details

Reaction catalysed: 
L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130451 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-seryl-tRNA(Sec) selenium transferase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 392 amino acids
Theoretical weight: 44.37 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67140 (Residues: 62-452; Coverage: 87%)
Gene names: aq_1031, selA
Sequence domains: L-seryl-tRNA selenium transferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PT 2 x PT
Ligand K 5 x K
2 modified residues:
Ligand MSE 80 x MSE
Ligand LLP 10 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A, SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 92.825Å b: 280.936Å c: 97.645Å
α: 90° β: 113.45° γ: 90°
R-values:
R R work R free
0.177 0.174 0.235
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Selenoproteins: molecular pathways and physiological roles.
Labunskyy et al. (2014)
9 more

1 mention without citation

Decameric SelA•tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation.
Itoh et al. (2013)