› 3b5i

X-ray diffraction
2.75Å resolution

Crystal structure of Indole-3-acetic Acid Methyltransferase

Released:
DOI: 10.2210/pdb3b5i/pdb
PDB entry 3b5i coloured by chain, front view.
PDB entry 3b5i coloured by chain, side view.
PDB entry 3b5i coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural, biochemical, and phylogenetic analyses suggest that indole-3-acetic acid methyltransferase is an evolutionarily ancient member of the SABATH family.
Zhao N, Ferrer JL, Ross J, Guan J, Yang Y, Pichersky E, Noel JP, Chen F
Plant Physiol 146 455-67 (2008)
PMID: 18162595

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + (indol-3-yl)acetate = S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190351 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Indole-3-acetate O-methyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 374 amino acids
Theoretical weight: 40.91 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9FLN8 (Residues: 13-386; Coverage: 97%)
Gene names: At5g55250, IAMT1, MCO15.20
Sequence domains: SAM dependent carboxyl methyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P21
Unit cell:
a: 67.27Å b: 129.4Å c: 68.33Å
α: 90° β: 112.3° γ: 90°
R-values:
R R work R free
0.258 0.257 0.282
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Phenylpropanoid biosynthesis.
Vogt T. (2010)
8 more

1 mention without citation

Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.
Lashley et al. (2022)