› 4p02

X-ray diffraction
2.65Å resolution

Structure of Bacterial Cellulose Synthase with cyclic-di-GMP bound.

Released:
DOI: 10.2210/pdb4p02/pdb
PDB entry 4p02 coloured by chain, front view.
PDB entry 4p02 coloured by chain, side view.
PDB entry 4p02 coloured by chain, top view.
Source organism: Cereibacter sphaeroides 2.4.1
Primary publication:
Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP.
Morgan JL, McNamara JT, Zimmer J
Nat Struct Mol Biol 21 489-96 (2014)
PMID: 24704788

Function and Biology Details

Reaction catalysed: 
UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-164971 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Cellulose synthase catalytic subunit [UDP-forming] Chain: A
Molecule details ›
Chain: A
Length: 803 amino acids
Theoretical weight: 90.01 KDa
Source organism: Cereibacter sphaeroides 2.4.1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3J125 (Residues: 2-788; Coverage: 100%)
Gene name: RSP_0333
Sequence domains:
Structure domains:
Cyclic di-GMP-binding protein Chain: B
Molecule details ›
Chain: B
Length: 724 amino acids
Theoretical weight: 76.64 KDa
Source organism: Cereibacter sphaeroides 2.4.1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3J126 (Residues: 1-724; Coverage: 100%)
Gene name: RSP_0332
Sequence domains:
Structure domains:
unidentified peptide Chain: D
Molecule details ›
Chain: D
Length: 9 amino acids
Theoretical weight: 784 Da
Source organism: Cereibacter sphaeroides 2.4.1
Expression system: Escherichia coli

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
4 bound ligands:
Ligand C2E 2 x C2E
Ligand PLC 4 x PLC
Ligand 3PE 1 x 3PE
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 67.64Å b: 214.66Å c: 220.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.23
Expression system: Escherichia coli

Quick links

Citations

28 review citations

Cyclic di-GMP: second messenger extraordinaire.
Jenal et al. (2017)
27 more

22 mentions without citation

Bacterial cellulose biosynthesis: diversity of operons, subunits, products, and functions.
Römling et al. (2015)
21 more