› 4acb

X-ray diffraction
3.34Å resolution

CRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METHANOCOCCUS MARIPALUDIS IN COMPLEX WITH THE GTP ANALOGUE GPPNHP

Released:
DOI: 10.2210/pdb4acb/pdb
PDB entry 4acb coloured by chain, front view.
PDB entry 4acb coloured by chain, side view.
PDB entry 4acb coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors.
Leibundgut M, Frick C, Thanbichler M, Böck A, Ban N
EMBO J 24 11-22 (2005)
PMID: 15616587

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Selenocysteine-specific elongation factor Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 482 amino acids
Theoretical weight: 54.15 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8J307 (Residues: 1-468; Coverage: 100%)
Gene names: MMJJ_15030, selB
Sequence domains:
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand GNP 1 x GNP
Ligand MG 2 x MG
Ligand GDP 1 x GDP
Ligand SO4 6 x SO4
Ligand DXC 7 x DXC
Ligand 5GP 1 x 5GP
1 modified residue:
Ligand CMH 16 x CMH

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3112
Unit cell:
a: 146.63Å b: 146.63Å c: 297.22Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

16 review citations

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

5 mentions without citation

Engineering the elongation factor Tu for efficient selenoprotein synthesis.
Haruna et al. (2014)
4 more