› 4s2a

X-ray diffraction
2.93Å resolution

Crystal structure of Caulobacter crescentus ThiC with Fe4S4 cluster at remote site (holo form)

Released:
DOI: 10.2210/pdb4s2a/pdb
PDB entry 4s2a coloured by chain, front view.
PDB entry 4s2a coloured by chain, side view.
PDB entry 4s2a coloured by chain, top view.
Source organism: Caulobacter vibrioides CB15
Primary publication:
Non-canonical active site architecture of the radical SAM thiamin pyrimidine synthase.
Fenwick MK, Mehta AP, Zhang Y, Abdelwahed SH, Begley TP, Ealick SE
Nat Commun 6 6480 (2015)
PMID: 25813242

Function and Biology Details

Reaction catalysed: 
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphomethylpyrimidine synthase Chain: A
Molecule details ›
Chain: A
Length: 614 amino acids
Theoretical weight: 68.25 KDa
Source organism: Caulobacter vibrioides CB15
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9A6Q5 (Residues: 1-612; Coverage: 100%)
Gene names: CC_2029, thiC
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand SF4 1 x SF4
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 116.657Å b: 68.922Å c: 97.62Å
α: 90° β: 120.3° γ: 90°
R-values:
R R work R free
0.197 0.194 0.246
Expression system: Escherichia coli

Quick links

Citations

6 review citations

C-C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products.
Yokoyama et al. (2018)
5 more

1 mention without citation

Non-canonical active site architecture of the radical SAM thiamin pyrimidine synthase.
Fenwick et al. (2015)