X-ray diffraction
3.03Å resolution

Crystal structure of folate-bound corrinoid iron-sulfur protein (CFeSP) in complex with its methyltransferase (MeTr), co-crystallized with folate and Ti(III) citrate reductant


Function and Biology Details

Reaction catalysed:
A [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 28.64 KDa
Source organism: Moorella thermoacetica
Expression system: Escherichia coli
  • Canonical: Q46389 (Residues: 1-262; Coverage: 100%)
Gene name: acsE
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like
Corrinoid/iron-sulfur protein large subunit Chains: C, E
Molecule details ›
Chains: C, E
Length: 446 amino acids
Theoretical weight: 48.21 KDa
Source organism: Moorella thermoacetica
  • Canonical: Q07340 (Residues: 1-446; Coverage: 100%)
Gene name: acsC
Sequence domains:
Structure domains:
Corrinoid/iron-sulfur protein small subunit Chains: D, F
Molecule details ›
Chains: D, F
Length: 323 amino acids
Theoretical weight: 35.11 KDa
Source organism: Moorella thermoacetica
  • Canonical: Q07341 (Residues: 1-323; Coverage: 100%)
Gene name: acsD
Sequence domains: CO dehydrogenase/acetyl-CoA synthase delta subunit
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

Cofactor: Ligand COB 2 x COB
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21212
Unit cell:
a: 136.006Å b: 250.686Å c: 81.8Å
α: 90° β: 90° γ: 90°
R R work R free
0.271 0.269 0.308
Expression system: Escherichia coli