› 4xvz

X-ray diffraction
2.49Å resolution

MycF mycinamicin III 3'-O-methyltransferase in complex with Mg

Released:
DOI: 10.2210/pdb4xvz/pdb
PDB entry 4xvz coloured by chain, front view.
PDB entry 4xvz coloured by chain, side view.
PDB entry 4xvz coloured by chain, top view.
Source organism: Micromonospora griseorubida
Primary publication:
Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases.
Bernard SM, Akey DL, Tripathi A, Park SR, Konwerski JR, Anzai Y, Li S, Kato F, Sherman DH, Smith JL
ACS Chem Biol 10 1340-51 (2015)
PMID: 25692963

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mycinamicin III 3''-O-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 283 amino acids
Theoretical weight: 32.16 KDa
Source organism: Micromonospora griseorubida
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q49492 (Residues: 2-254; Coverage: 100%)
Gene name: mycF
Sequence domains: Macrocin-O-methyltransferase (TylF)

Ligands and Environments

2 bound ligands:
Ligand CL 4 x CL
Ligand MG 4 x MG
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 123.864Å b: 148.587Å c: 66.855Å
α: 90° β: 120.23° γ: 90°
R-values:
R R work R free
0.18 0.178 0.217
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Methyltransferases: Functions and Applications.
Abdelraheem et al. (2022)
6 other articles

1 mention without citation

Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases.
Bernard et al. (2015)