› 2nt8

X-ray diffraction
1.68Å resolution

ATP bound at the active site of a PduO type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri

Released:
DOI: 10.2210/pdb2nt8/pdb
PDB entry 2nt8 coloured by chain, front view.
PDB entry 2nt8 coloured by chain, side view.
PDB entry 2nt8 coloured by chain, top view.
Source organism: Limosilactobacillus reuteri
Primary publication:
Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri.
St Maurice M, Mera PE, Taranto MP, Sesma F, Escalante-Semerena JC, Rayment I
J Biol Chem 282 2596-605 (2007)
PMID: 17121823

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: 223 amino acids
Theoretical weight: 25.64 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 MG 1 x MG
Ligand SO4 1 x SO4
Ligand ATP 1 x ATP
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I23
Unit cell:
a: 110.609Å b: 110.609Å c: 110.609Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.204
Expression system: Escherichia coli

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Citations

7 review citations

Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials.
Apostolovic et al. (2010)
6 more

3 mentions without citation

Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate.
St Maurice et al. (2008)
2 more