› 4jc0

X-ray diffraction
3.3Å resolution

Crystal structure of Thermotoga maritima holo RimO in complex with pentasulfide, Northeast Structural Genomics Consortium Target VR77

Released:
DOI: 10.2210/pdb4jc0/pdb
PDB entry 4jc0 coloured by chain, front view.
PDB entry 4jc0 coloured by chain, side view.
PDB entry 4jc0 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases.
Forouhar F, Arragain S, Atta M, Gambarelli S, Mouesca JM, Hussain M, Xiao R, Kieffer-Jaquinod S, Seetharaman J, Acton TB, Montelione GT, Mulliez E, Hunt JF, Fontecave M
Nat Chem Biol 9 333-8 (2013)
PMID: 23542644

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + L-aspartate(89)-[ribosomal protein S12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate(89)-[ribosomal protein S12]-methanethiol + (sulfur carrier)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194895 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal protein uS12 methylthiotransferase RimO Chains: A, B
Molecule details ›
Chains: A, B
Length: 438 amino acids
Theoretical weight: 50.36 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X2H6 (Residues: 1-430; Coverage: 100%)
Gene names: TM_1862, rimO
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FS5 2 x FS5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 59.721Å b: 86.948Å c: 172.795Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.245 0.296
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

22 review citations

Radical S-Adenosylmethionine Enzymes in Human Health and Disease.
Landgraf et al. (2016)
21 more

7 mentions without citation

Radical S-adenosylmethionine enzymes.
Broderick et al. (2014)
6 more