8xj3

X-ray diffraction
2.3Å resolution

Crystal structure of methyltransferase CbiL from Akkermansia muciniphila

Released:
Source organism: Akkermansia muciniphila
Primary publication:
Crystal structure of methyltransferase CbiL from Akkermansia muciniphila.
Biochem Biophys Res Commun 722 150165 (2024)
PMID: 38805786

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-246764 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cobalt-precorrin-2 C(20)-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 28.33 KDa
Source organism: Akkermansia muciniphila
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A6N2RW51 (Residues: 1-235; Coverage: 100%)
Gene names: AMLFYP55_01830, cbiL
Sequence domains: Tetrapyrrole (Corrin/Porphyrin) Methylases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P212121
Unit cell:
a: 55.413Å b: 62.76Å c: 131.419Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.24
Expression system: Escherichia coli BL21(DE3)