› 4a2n

X-ray diffraction
3.4Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-S-isoprenylcysteine O-methyltransferase Chain: B
Molecule details ›
Chain: B
Length: 194 amino acids
Theoretical weight: 22.84 KDa
Source organism: Methanosarcina acetivorans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8TMG0 (Residues: 1-194; Coverage: 100%)
Gene name: MA_2698
Sequence domains: Isoprenylcysteine carboxyl methyltransferase (ICMT) family
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
2 bound ligands:
Ligand PLM 1 x PLM
Ligand CDL 1 x CDL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P6222
Unit cell:
a: 114.92Å b: 114.92Å c: 169.291Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.238 0.275
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Protein prenylation: unique fats make their mark on biology.
Wang et al. (2016)
5 more

17 mentions without citation

Structural basis for catalysis at the membrane-water interface.
Dufrisne et al. (2017)
16 more