› 2vnl

X-ray diffraction
1.8Å resolution

MUTANT Y108Wdel OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C- TERMINally fused to ISOLEUCINE ZIPPER pIIGCN4 (chimera II)

Released:
DOI: 10.2210/pdb2vnl/pdb
PDB entry 2vnl coloured by chain, front view.
PDB entry 2vnl coloured by chain, side view.
PDB entry 2vnl coloured by chain, top view.
Source organisms:
Primary publication:
Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker.
Seul A, Müller JJ, Andres D, Stettner E, Heinemann U, Seckler R
Acta Crystallogr D Biol Crystallogr 70 1336-45 (2014)
PMID: 24816102

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control transcription factor GCN4; Tail spike protein Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 16.88 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12528 (Residues: 2-123; Coverage: 18%)
  • Canonical: P03069 (Residues: 252-280; Coverage: 10%)
Gene names: 9, AAS101, AAS3, ARG9, GCN4, YEL009C
Sequence domains:
Structure domains: Phage P22 tailspike-like, N-terminal domain

Ligands and Environments

1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: R3
Unit cell:
a: 58.012Å b: 58.012Å c: 156.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.229
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Targeting mechanisms of tailed bacteriophages.
Nobrega et al. (2018)
1 more