› 2ylk

X-ray diffraction
2.2Å resolution

Carbohydrate-binding module CBM3b from the cellulosomal cellobiohydrolase 9A from Clostridium thermocellum

Released:
DOI: 10.2210/pdb2ylk/pdb
PDB entry 2ylk coloured by chain, front view.
PDB entry 2ylk coloured by chain, side view.
PDB entry 2ylk coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
A single mutation reforms the binding activity of an adhesion-deficient family 3 carbohydrate-binding module.
Yaniv O, Petkun S, Shimon LJ, Bayer EA, Lamed R, Frolow F
Acta Crystallogr D Biol Crystallogr 68 819-28 (2012)
PMID: 22751667

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176793 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucanase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 145 amino acids
Theoretical weight: 16.56 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q59325 (Residues: 1004-1147; Coverage: 12%)
Gene name: cbhA
Sequence domains: Cellulose binding domain
Structure domains: Endoglucanase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41
Unit cell:
a: 95.456Å b: 95.456Å c: 82.911Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.226
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Thermophilic lignocellulose deconstruction.
Blumer-Schuette et al. (2014)
1 more

1 mention without citation

Novel clostridial cell-surface hemicellulose-binding CBM3 proteins.
Hershko Rimon et al. (2021)