› 7xig

X-ray diffraction
2.25Å resolution

Crystal structure of the aminopropyltransferase, SpeE from hyperthermophilic crenarchaeon, Pyrobaculum calidifontis in complex with 5'-methylthioadenosine (MTA) and spermine

Released:
DOI: 10.2210/pdb7xig/pdb
PDB entry 7xig coloured by chain, front view.
PDB entry 7xig coloured by chain, side view.
PDB entry 7xig coloured by chain, top view.
Source organism: Pyrobaculum calidifontis
Primary publication:
Substrate Specificity of an Aminopropyltransferase and the Biosynthesis Pathway of Polyamines in the Hyperthermophilic Crenarchaeon Pyrobaculum calidifontis.
Fukuda W, Osaki M, Yasuda Y, Hidese R, Higuchi T, Umezawa N, Fujiwara S, Mizohata E
Catalysts 12 (2022)

Function and Biology Details

Reaction catalysed: 
S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyamine aminopropyltransferase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 309 amino acids
Theoretical weight: 34.86 KDa
Source organism: Pyrobaculum calidifontis
Expression system: Escherichia coli
UniProt:
  • Canonical: A3MU81 (Residues: 1-289; Coverage: 100%)
Gene names: Pcal_0772, speE
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand MTA 8 x MTA
Ligand SPM 8 x SPM
Ligand EPE 2 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P1
Unit cell:
a: 77.828Å b: 80.392Å c: 97.844Å
α: 72.46° β: 89.13° γ: 88.08°
R-values:
R R work R free
0.174 0.173 0.207
Expression system: Escherichia coli

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