› 8rtc

X-ray diffraction
2.83Å resolution

Rap from bacteriophage Phi3T in presence of pheromone RGHTS

Released:
DOI: 10.2210/pdb8rtc/pdb
PDB entry 8rtc coloured by chain, front view.
PDB entry 8rtc coloured by chain, side view.
PDB entry 8rtc coloured by chain, top view.
Source organism: Bacillus phage phi3T
Primary publication:
Extracellular proteolysis of tandemly duplicated pheromone propeptides affords additional complexity to bacterial quorum sensing.
Felipe-Ruiz A, Zamora-Caballero S, Bendori SO, Penadés JR, Eldar A, Marina A
PLoS Biol 22 e3002744 (2024)
PMID: 39137235

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-247239 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Rap3T Chains: A, B
Molecule details ›
Chains: A, B
Length: 379 amino acids
Theoretical weight: 45.03 KDa
Source organism: Bacillus phage phi3T
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1P8CWN8 (Residues: 1-379; Coverage: 100%)
Gene name: phi3T_14
Sequence domains:
Pheromone RGHTS Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 amino acids
Theoretical weight: 559 Da
Source organism: Bacillus phage phi3T
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand A1H22 4 x A1H22
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21
Unit cell:
a: 60.6Å b: 92.66Å c: 101.97Å
α: 90° β: 107.07° γ: 90°
R-values:
R R work R free
0.23 0.228 0.267
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

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