› 2qgq

X-ray diffraction
2Å resolution

Crystal structure of TM_1862 from Thermotoga maritima. Northeast Structural Genomics Consortium target VR77

Released:
DOI: 10.2210/pdb2qgq/pdb
PDB entry 2qgq coloured by chain, front view.
PDB entry 2qgq coloured by chain, side view.
PDB entry 2qgq coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase.
Arragain S, Garcia-Serres R, Blondin G, Douki T, Clemancey M, Latour JM, Forouhar F, Neely H, Montelione GT, Hunt JF, Mulliez E, Fontecave M, Atta M
J Biol Chem 285 5792-801 (2010)
PMID: 20007320

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, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 304 amino acids
Theoretical weight: 35.46 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X2H6 (Residues: 135-430; Coverage: 69%)
Gene names: TM_1862, rimO
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CXS 4 x CXS
1 modified residue:
Ligand MSE 48 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 88.62Å b: 88.649Å c: 96.039Å
α: 89.98° β: 90.03° γ: 89.91°
R-values:
R R work R free
0.212 0.212 0.251
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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

7 mentions without citation

Structural insights into radical generation by the radical SAM superfamily.
Vey et al. (2011)
6 more