› 2qtt

X-ray diffraction
1.93Å resolution

Crystal Structure of Arabidopsis thaliana 5'-Methylthioadenosine nucleosidase in complex with Formycin A

Released:
DOI: 10.2210/pdb2qtt/pdb
PDB entry 2qtt coloured by chain, front view.
PDB entry 2qtt coloured by chain, side view.
PDB entry 2qtt coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Molecular determinants of substrate specificity in plant 5'-methylthioadenosine nucleosidases.
Siu KK, Lee JE, Sufrin JR, Moffatt BA, McMillan M, Cornell KA, Isom C, Howell PL
J Mol Biol 378 112-28 (2008)
PMID: 18342331

Function and Biology Details

Reaction catalysed: 
S-methyl-5'-thioadenosine + H(2)O = 5-(methylsulfanyl)-D-ribose + adenine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5'-methylthioadenosine nucleosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 28.48 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9T0I8 (Residues: 1-267; Coverage: 100%)
Gene names: At4g38800, MTAN, MTAN1, MTN1, T9A14.80
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

3 bound ligands:
Ligand ADE 1 x ADE
Ligand EDO 1 x EDO
Ligand FMC 1 x FMC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300, null
Spacegroup: P21
Unit cell:
a: 41.3Å b: 127.05Å c: 45.45Å
α: 90° β: 109.63° γ: 90°
R-values:
R R work R free
0.178 0.172 0.233
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5'-methylthioadenosine.
Albers E. (2009)
9 other articles

2 mentions without citation

Molecular determinants of substrate specificity in plant 5'-methylthioadenosine nucleosidases.
Siu et al. (2008)
1 more