› 1m6e

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF SALICYLIC ACID CARBOXYL METHYLTRANSFERASE (SAMT)

Released:
DOI: 10.2210/pdb1m6e/pdb
PDB entry 1m6e coloured by chain, front view.
PDB entry 1m6e coloured by chain, side view.
PDB entry 1m6e coloured by chain, top view.
Source organism: Clarkia breweri
Primary publication:
Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family.
Zubieta C, Ross JR, Koscheski P, Yang Y, Pichersky E, Noel JP
Plant Cell 15 1704-16 (2003)
PMID: 12897246

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + salicylate = S-adenosyl-L-homocysteine + methyl salicylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193501 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Salicylate carboxymethyltransferase Chain: X
Molecule details ›
Chain: X
Length: 359 amino acids
Theoretical weight: 40.33 KDa
Source organism: Clarkia breweri
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SPV4 (Residues: 1-359; Coverage: 100%)
Gene name: SAMT
Sequence domains: SAM dependent carboxyl methyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
2 bound ligands:
Ligand LU 1 x LU
Ligand SAL 1 x SAL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A, null
Spacegroup: P43212
Unit cell:
a: 141.74Å b: 141.74Å c: 63.983Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.288
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Auxin: regulation, action, and interaction.
Woodward et al. (2005)
19 more

6 mentions without citation

Enzyme action in the regulation of plant hormone responses.
Westfall et al. (2013)
5 more