› 5cxu

X-ray diffraction
1.6Å resolution

Structure of the CE1 ferulic acid esterase AmCE1/Fae1A, from the anaerobic fungi Anaeromyces mucronatus in the absence of substrate

Released:
DOI: 10.2210/pdb5cxu/pdb
PDB entry 5cxu coloured by chain, front view.
PDB entry 5cxu coloured by chain, side view.
PDB entry 5cxu coloured by chain, top view.
Source organism: Anaeromyces mucronatus
Primary publication:
Contributions of a unique β-clamp to substrate recognition illuminates the molecular basis of exolysis in ferulic acid esterases.
Gruninger RJ, Cote C, McAllister TA, Abbott DW
Biochem J 473 839-49 (2016)
PMID: 27026397

Function and Biology Details

Reaction catalysed: 
Feruloyl-polysaccharide + H(2)O = ferulate + polysaccharide
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fae1A Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 31.08 KDa
Source organism: Anaeromyces mucronatus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F2YCB6 (Residues: 1-275; Coverage: 100%)
Gene name: fae1A
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: I4
Unit cell:
a: 101.87Å b: 101.87Å c: 52.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.14 0.165
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Decoding the roles of extremophilic microbes in the anaerobic environments: Past, Present, and Future.
Patidar et al. (2022)
1 more

1 mention without citation

Structure and enzymatic characterization of CelD endoglucanase from the anaerobic fungus Piromyces finnis.
Dementiev et al. (2023)