› 3gah

X-ray diffraction
1.17Å resolution

Structure of a F112H variant PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri complexed with cobalamin and ATP

Released:
DOI: 10.2210/pdb3gah/pdb
PDB entry 3gah coloured by chain, front view.
PDB entry 3gah coloured by chain, side view.
PDB entry 3gah coloured by chain, top view.
Source organism: Limosilactobacillus reuteri
Primary publication:
Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme.
Mera PE, St Maurice M, Rayment I, Escalante-Semerena JC
Biochemistry 48 3138-45 (2009)
PMID: 19236001

Function and Biology Details

Reaction catalysed: 
(1a) 2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Corrinoid adenosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 22.37 KDa
Source organism: Limosilactobacillus reuteri
Expression system: Escherichia coli
UniProt:
  • Canonical: Q50EJ2 (Residues: 2-188; Coverage: 100%)
Gene names: GIX77_03270, cobA
Sequence domains: Cobalamin adenosyltransferase
Structure domains: Cobalamin adenosyltransferase-like

Ligands and Environments

4 bound ligands:
Ligand ATP 1 x ATP
Ligand B12 1 x B12
Ligand MG 2 x MG
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: R3
Unit cell:
a: 80.814Å b: 80.814Å c: 89.492Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.16 0.182
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Diverse bacterial microcompartment organelles.
Chowdhury et al. (2014)
3 more

2 mentions without citation

Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme.
Mera et al. (2009)
1 more