› 3wco

X-ray diffraction
2.4Å resolution

Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA

Released:
DOI: 10.2210/pdb3wco/pdb
PDB entry 3wco coloured by chain, front view.
PDB entry 3wco coloured by chain, side view.
PDB entry 3wco coloured by chain, top view.
Source organism: Aquifex aeolicus VF5
Primary publication:
Dimer-dimer interaction of the bacterial selenocysteine synthase SelA promotes functional active-site formation and catalytic specificity.
Itoh Y, Bröcker MJ, Sekine S, Söll D, Yokoyama S
J Mol Biol 426 1723-35 (2014)
PMID: 24456689

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-seryl-tRNA(Sec) selenium transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 392 amino acids
Theoretical weight: 44.47 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67140 (Residues: 61-452; Coverage: 87%)
Gene names: aq_1031, selA
Sequence domains: L-seryl-tRNA selenium transferase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand THJ 5 x THJ
2 modified residues:
Ligand MSE 16 x MSE
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 59.19Å b: 81.286Å c: 95.537Å
α: 90° β: 92.23° γ: 90°
R-values:
R R work R free
0.181 0.179 0.229
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The unique tRNASec and its role in selenocysteine biosynthesis.
Serrão et al. (2018)
1 more

2 mentions without citation

Dimer-dimer interaction of the bacterial selenocysteine synthase SelA promotes functional active-site formation and catalytic specificity.
Itoh et al. (2014)
1 more