› 5nrk

X-ray diffraction
1.45Å resolution

Crystal structure of the sixth cohesin from Acetivibrio cellulolyticus' scaffoldin B in complex with Cel5 dockerin S15I, I16N mutant

Released:
DOI: 10.2210/pdb5nrk/pdb
PDB entry 5nrk coloured by chain, front view.
PDB entry 5nrk coloured by chain, side view.
PDB entry 5nrk coloured by chain, top view.
Source organism: Acetivibrio cellulolyticus
Primary publication:
Structure-function analyses generate novel specificities to assemble the components of multienzyme bacterial cellulosome complexes.
Bule P, Cameron K, Prates JAM, Ferreira LMA, Smith SP, Gilbert HJ, Bayer EA, Najmudin S, Fontes CMGA, Alves VD
J Biol Chem 293 4201-4212 (2018)
PMID: 29367338

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-496861 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Endoglucanase Chains: A, C
Molecule details ›
Chains: A, C
Length: 143 amino acids
Theoretical weight: 14.75 KDa
Source organism: Acetivibrio cellulolyticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RPL0 (Residues: 1472-1611; Coverage: 7%)
Gene name: cipV
Sequence domains: Cohesin domain
Dockerin domain-containing protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 68 amino acids
Theoretical weight: 7.49 KDa
Source organism: Acetivibrio cellulolyticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A2R2JFJ6 (Residues: 1-68; Coverage: 100%)
Gene name: BglC
Sequence domains: Dockerin type I domain
Structure domains: Dockerin domain

Ligands and Environments

3 bound ligands:
Ligand CA 6 x CA
Ligand SCN 3 x SCN
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 46.539Å b: 79.809Å c: 112.159Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.144 0.17
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Research progress and the biotechnological applications of multienzyme complex.
Jiang et al. (2021)
1 more

1 mention without citation

Structure-function analyses generate novel specificities to assemble the components of multienzyme bacterial cellulosome complexes.
Bule et al. (2018)