› 3bwz

X-ray diffraction
1.2Å resolution

Crystal structure of the type II cohesin module from the cellulosome of Acetivibrio cellulolyticus with an extended linker conformation

Released:
DOI: 10.2210/pdb3bwz/pdb
PDB entry 3bwz coloured by chain, front view.
PDB entry 3bwz coloured by chain, side view.
PDB entry 3bwz coloured by chain, top view.
Source organism: Acetivibrio cellulolyticus
Primary publication:
Intermodular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus.
Noach I, Frolow F, Alber O, Lamed R, Shimon LJ, Bayer EA
J Mol Biol 391 86-97 (2009)
PMID: 19501595

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-182160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dockerin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 19.59 KDa
Source organism: Acetivibrio cellulolyticus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7WYN3 (Residues: 28-199; Coverage: 18%)
Gene name: scaB
Sequence domains: Cohesin domain
Structure domains: Immunoglobulin-like

Ligands and Environments

3 bound ligands:
Ligand NO3 1 x NO3
Ligand CL 3 x CL
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 37.455Å b: 55.78Å c: 87.912Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.124 0.122 0.152
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Applications of computational science for understanding enzymatic deconstruction of cellulose.
Beckham et al. (2011)
16 other articles

1 mention without citation

A dual cohesin-dockerin complex binding mode in Bacteroides cellulosolvens contributes to the size and complexity of its cellulosome.
Duarte et al. (2021)