› 3ssm

X-ray diffraction
2.25Å resolution

MycE Methyltransferase from the Mycinamycin Biosynthetic Pathway in Complex with Mg and SAH, Crystal form 1

Released:
DOI: 10.2210/pdb3ssm/pdb
PDB entry 3ssm coloured by chain, front view.
PDB entry 3ssm coloured by chain, side view.
PDB entry 3ssm coloured by chain, top view.
Source organism: Micromonospora griseorubida
Primary publication:
A new structural form in the SAM/metal-dependent o‑methyltransferase family: MycE from the mycinamicin biosynthetic pathway.
Akey DL, Li S, Konwerski JR, Confer LA, Bernard SM, Anzai Y, Kato F, Sherman DH, Smith JL
J Mol Biol 413 438-50 (2011)
PMID: 21884704

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + mycinamicin VI = S-adenosyl-L-homocysteine + mycinamicin III
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mycinamicin VI 2''-O-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 419 amino acids
Theoretical weight: 47.04 KDa
Source organism: Micromonospora griseorubida
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83WF2 (Residues: 1-399; Coverage: 100%)
Gene name: mycE
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand SAH 3 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 73.914Å b: 143.407Å c: 84.641Å
α: 90° β: 105.6° γ: 90°
R-values:
R R work R free
0.167 0.165 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
2 more

2 mentions without citation

Structure-function-guided exploration of the antimicrobial peptide polybia-CP identifies activity determinants and generates synthetic therapeutic candidates.
Torres et al. (2018)
1 more