› 1m6y

X-ray diffraction
1.9Å resolution

Crystal Structure Analysis of TM0872, a Putative SAM-dependent Methyltransferase, Complexed with SAH

Released:
DOI: 10.2210/pdb1m6y/pdb
PDB entry 1m6y coloured by chain, front view.
PDB entry 1m6y coloured by chain, side view.
PDB entry 1m6y coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Crystal complexes of a predicted S-adenosylmethionine-dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain.
Miller DJ, Ouellette N, Evdokimova E, Savchenko A, Edwards A, Anderson WF
Protein Sci 12 1432-42 (2003)
PMID: 12824489

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + cytosine(1402) in 16S rRNA = S-adenosyl-L-homocysteine + N(4)-methylcytosine(1402) in 16S rRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194651 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal RNA small subunit methyltransferase H Chains: A, B
Molecule details ›
Chains: A, B
Length: 301 amino acids
Theoretical weight: 35.38 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9WZX6 (Residues: 1-299; Coverage: 100%)
Gene names: TM_0872, mraW, rsmH
Sequence domains: MraW methylase family
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
Ligand SO4 2 x SO4
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P213
Unit cell:
a: 133.4Å b: 133.4Å c: 133.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
5 more

7 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
6 more