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8RSV

Rap from bacteriophage Phi3T in presence of pheromone RRGHTAS

This is a non-PDB format compatible entry.
Summary for 8RSV
Entry DOI10.2210/pdb8rsv/pdb
Related8RSU 8rst
DescriptorRap3T, Pheromone RRGHTAS, Glycerol ethoxylate, ... (4 entities in total)
Functional Keywordsrap, aspartate phosphatase, phi3t, bacteriophage, signaling protein
Biological sourceBacillus phage phi3T
More
Total number of polymer chains4
Total formula weight93400.25
Authors
Felipe-Ruiz, A.,Zamora-Caballero, S.,Marina, A. (deposition date: 2024-01-25, release date: 2024-07-24, Last modification date: 2024-08-28)
Primary citationFelipe-Ruiz, A.,Zamora-Caballero, S.,Bendori, S.O.,Penades, J.R.,Eldar, A.,Marina, A.
Extracellular proteolysis of tandemly duplicated pheromone propeptides affords additional complexity to bacterial quorum sensing.
Plos Biol., 22:e3002744-e3002744, 2024
Cited by
PubMed Abstract: Bacterial interactions are vital for adapting to changing environments, with quorum sensing (QS) systems playing a central role in coordinating behaviors through small signaling molecules. The RRNPPA family is the prevalent QS systems in Bacillota and mediating communication through secreted oligopeptides, which are processed into active pheromones by extracellular proteases. Notably, in several cases the propeptides show the presence of multiple putative pheromones within their sequences, which has been proposed as a mechanism to diversify peptide-receptor specificity and potentially facilitate new functions. However, neither the processes governing the maturation of propeptides containing multiple pheromones, nor their functional significance has been evaluated. Here, using 2 Rap systems from bacteriophages infecting Bacillus subtilis that exhibit different types of pheromone duplication in their propeptides, we investigate the maturation process and the molecular and functional activities of the produced pheromones. Our results reveal that distinct maturation processes generate multiple mature pheromones, which bind to receptors with varying affinities but produce identical structural and biological responses. These findings add additional layers in the complexity of QS communication and regulation, opening new possibilities for microbial social behaviors, highlighting the intricate nature of bacterial interactions and adaptation.
PubMed: 39137235
DOI: 10.1371/journal.pbio.3002744
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.19 Å)
Structure validation

227111

数据于2024-11-06公开中

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