› 3gw6

X-ray diffraction
2.6Å resolution

Intramolecular Chaperone

Released:
DOI: 10.2210/pdb3gw6/pdb
PDB entry 3gw6 coloured by chain, front view.
PDB entry 3gw6 coloured by chain, side view.
PDB entry 3gw6 coloured by chain, top view.
Source organism: Escherichia phage K1F
Primary publication:
Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding.
Schulz EC, Dickmanns A, Urlaub H, Schmitt A, Mühlenhoff M, Stummeyer K, Schwarzer D, Gerardy-Schahn R, Ficner R
Nat Struct Mol Biol 17 210-5 (2010)
PMID: 20118935

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mature tail spike protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 275 amino acids
Theoretical weight: 30.71 KDa
Source organism: Escherichia phage K1F
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04830 (Residues: 790-1064; Coverage: 26%)
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand PEG 18 x PEG
Ligand TAM 3 x TAM
Ligand CL 6 x CL
Ligand BR 6 x BR
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P1
Unit cell:
a: 62.65Å b: 79.95Å c: 109.58Å
α: 81.71° β: 76.53° γ: 87.11°
R-values:
R R work R free
0.211 0.209 0.254
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Bacteriophage protein-protein interactions.
Häuser et al. (2012)
2 more

21 mentions without citation

Bioinformatics perspective on rhomboid intramembrane protease evolution and function.
Kinch et al. (2013)
20 more