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TitleExtracellular proteolysis of tandemly duplicated pheromone propeptides affords additional complexity to bacterial quorum sensing.
Journal, issue, pagesPlos Biol., Vol. 22, Page e3002744-e3002744, Year 2024
Publish dateJan 25, 2024 (structure data deposition date)
AuthorsFelipe-Ruiz, A. / Zamora-Caballero, S. / Bendori, S.O. / Penades, J.R. / Eldar, A. / Marina, A.
External linksPlos Biol. / PubMed:39137235
MethodsX-ray diffraction
Resolution2.19 - 2.83 Å
Structure data

PDB-8rst:
Rap from bacteriophage Phi3T in presence of pheromone SRGHTS
Method: X-RAY DIFFRACTION / Resolution: 2.56 Å

PDB-8rsu:
Rap from bacteriophage Phi3T in presence of pheromone RRGHTA
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-8rsv:
Rap from bacteriophage Phi3T in presence of pheromone RRGHTAS
Method: X-RAY DIFFRACTION / Resolution: 2.19 Å

PDB-8rtc:
Rap from bacteriophage Phi3T in presence of pheromone RGHTS
Method: X-RAY DIFFRACTION / Resolution: 2.83 Å

PDB-8rte:
Rap from bacteriophage Phi105 with peptide ERPVGT
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

PDB-1h22:
Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(10)-hupyridone at 2.15A resolution

ChemComp-FU1:
tetrahydrofuran

ChemComp-HOH:
WATER

Source
  • bacillus phage phi3t (virus)
  • bacillus phage phi105 (virus)
KeywordsSIGNALING PROTEIN / Rap / Aspartate phosphatase / Phi3T / Bacteriophage

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