› 1tlu

X-ray diffraction
1.55Å resolution

Crystal Structure of Thermotoga maritima S-adenosylmethionine decarboxylase

Released:
DOI: 10.2210/pdb1tlu/pdb
PDB entry 1tlu coloured by chain, front view.
PDB entry 1tlu coloured by chain, side view.
PDB entry 1tlu coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase.
Toms AV, Kinsland C, McCloskey DE, Pegg AE, Ealick SE
J Biol Chem 279 33837-46 (2004)
PMID: 15150268

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine decarboxylase proenzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.81 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZC3 (Residues: 1-130; Coverage: 100%)
Gene names: TM_0655, speH
Sequence domains: S-adenosylmethionine decarboxylase
Structure domains: S-adenosylmethionine decarboxylase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: R3
Unit cell:
a: 104.994Å b: 104.994Å c: 69.695Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.152 0.187
Expression system: Escherichia coli

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Citations

3 review citations

Spermine synthase.
Pegg et al. (2010)
2 more

8 mentions without citation

Structural biology of S-adenosylmethionine decarboxylase.
Bale et al. (2010)
7 more