All peptides induce identical conformation in Rap3T

(a) RMSD calculation from the superimposition of Cα atoms of Rap3T structures in complex with peptides SRGHTS, RGHTS, RRGHTA, and RRGHTAS. RMSD were calculated from individual monomers (lower) and dimers (upper). Number of atoms used in RMSD calculation is showed between parenthesis. (b) Superpositi...

ver descrição completa

Detalhes bibliográficos
Autores: Felipe-Ruiz, Alonso, Zamora-Caballero, Sara, Bendori, Shira Omer, Penadés, José R., Eldar, Avigdor, Marina, Alberto
Formato: conjunto de datos
Estado:Versión publicada
Fecha de publicación:2024
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/372064
Acesso em linha:http://hdl.handle.net/10261/372064
Access Level:acceso abierto
Palavra-chave:Small signaling molecules
Produce identical structural
Opening new possibilities
Exhibit different types
Microbial social behaviors
Bacillus subtilis
Prevalent qs systems
Systems playing
Coordinating behaviors
Bacillota
Varying affinities
Several cases
Secreted oligopeptides
RRNPPA family
Results reveal
Receptor specificity
Quorum sensing
qs communication
Produced pheromones
Processes governing
Pheromone duplication
Mediating communication
Intricate nature
Functional significance
Functional activities
Extracellular proteolysis
Extracellular proteases
Diversify peptide
Changing environments
Central role
Biological responses
Bacteriophages infecting
Bacterial interactions
Active pheromones
Quorum Sensing
https://www.ncbi.nlm.nih.gov/mesh/68053038
https://www.ncbi.nlm.nih.gov/mesh/68001412
id ES_ffbf29bf17b3f1c9184e4f8d5b71e8a1
oai_identifier_str oai:digital.csic.es:10261/372064
network_acronym_str ES
network_name_str España
repository_id_str
spelling All peptides induce identical conformation in Rap3TFelipe-Ruiz, AlonsoZamora-Caballero, SaraBendori, Shira OmerPenadés, José R.Eldar, AvigdorMarina, AlbertoSmall signaling moleculesProduce identical structuralOpening new possibilitiesExhibit different typesMicrobial social behaviorsBacillus subtilisPrevalent qs systemsSystems playingCoordinating behaviorsBacillotaVarying affinitiesSeveral casesSecreted oligopeptidesRRNPPA familyResults revealReceptor specificityQuorum sensingqs communicationProduced pheromonesProcesses governingPheromone duplicationMediating communicationIntricate natureFunctional significanceFunctional activitiesExtracellular proteolysisExtracellular proteasesDiversify peptideChanging environmentsCentral roleBiological responsesBacteriophages infectingBacterial interactionsActive pheromonesQuorum SensingBacillus subtilishttps://www.ncbi.nlm.nih.gov/mesh/68053038https://www.ncbi.nlm.nih.gov/mesh/68001412(a) RMSD calculation from the superimposition of Cα atoms of Rap3T structures in complex with peptides SRGHTS, RGHTS, RRGHTA, and RRGHTAS. RMSD were calculated from individual monomers (lower) and dimers (upper). Number of atoms used in RMSD calculation is showed between parenthesis. (b) Superposition of 4 Rap3T-Peptide complexes with different pheromone variants in monomeric state RRGHTAS (blue), RRGHTA (pink), RGHTS (light green), and SRGHTS (orange). (c) Superposition of dimers for the 4 Rap3T complexes with peptides RRGHTAS (blue), RRGHTA (pink), RGHTS (light green), and SRGHTS (orange).pbio.3002744.s004.tiffPeer reviewedFigshareMarina, Alberto [0000-0002-1334-5273]Zamora-Caballero, Sara [0000-0003-4717-8845]Penadés, José R. [0000-0002-6439-5262]Felipe-Ruiz, Alonso [0000-0002-7335-5764]Marina, AlbertoConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242024info:eu-repo/semantics/datasethttp://purl.org/coar/resource_type/c_ddb1Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/372064reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésFelipe-Ruiz, Alonso; Zamora-Caballero, Sara; Bendori, Shira Omer; Penadés, José R.; Eldar, Avigdor; Marina, Alberto (2024) Extracellular proteolysis of tandemly duplicated pheromone propeptides affords additional complexity to bacterial quorum sensing. PLoS - Biology 22(8):e3002744. https://doi.org/10.1371/journal.pbio.3002744. http://hdl.handle.net/10261/368076https://doi.org/10.1371/journal.pbio.3002744.s004Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3720642026-05-22T06:33:51Z
dc.title.none.fl_str_mv All peptides induce identical conformation in Rap3T
title All peptides induce identical conformation in Rap3T
spellingShingle All peptides induce identical conformation in Rap3T
Felipe-Ruiz, Alonso
Small signaling molecules
Produce identical structural
Opening new possibilities
Exhibit different types
Microbial social behaviors
Bacillus subtilis
Prevalent qs systems
Systems playing
Coordinating behaviors
Bacillota
Varying affinities
Several cases
Secreted oligopeptides
RRNPPA family
Results reveal
Receptor specificity
Quorum sensing
qs communication
Produced pheromones
Processes governing
Pheromone duplication
Mediating communication
Intricate nature
Functional significance
Functional activities
Extracellular proteolysis
Extracellular proteases
Diversify peptide
Changing environments
Central role
Biological responses
Bacteriophages infecting
Bacterial interactions
Active pheromones
Quorum Sensing
Bacillus subtilis
https://www.ncbi.nlm.nih.gov/mesh/68053038
https://www.ncbi.nlm.nih.gov/mesh/68001412
title_short All peptides induce identical conformation in Rap3T
title_full All peptides induce identical conformation in Rap3T
title_fullStr All peptides induce identical conformation in Rap3T
title_full_unstemmed All peptides induce identical conformation in Rap3T
title_sort All peptides induce identical conformation in Rap3T
dc.creator.none.fl_str_mv Felipe-Ruiz, Alonso
Zamora-Caballero, Sara
Bendori, Shira Omer
Penadés, José R.
Eldar, Avigdor
Marina, Alberto
author Felipe-Ruiz, Alonso
author_facet Felipe-Ruiz, Alonso
Zamora-Caballero, Sara
Bendori, Shira Omer
Penadés, José R.
Eldar, Avigdor
Marina, Alberto
author_role author
author2 Zamora-Caballero, Sara
Bendori, Shira Omer
Penadés, José R.
Eldar, Avigdor
Marina, Alberto
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Marina, Alberto [0000-0002-1334-5273]
Zamora-Caballero, Sara [0000-0003-4717-8845]
Penadés, José R. [0000-0002-6439-5262]
Felipe-Ruiz, Alonso [0000-0002-7335-5764]
Marina, Alberto
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Small signaling molecules
Produce identical structural
Opening new possibilities
Exhibit different types
Microbial social behaviors
Bacillus subtilis
Prevalent qs systems
Systems playing
Coordinating behaviors
Bacillota
Varying affinities
Several cases
Secreted oligopeptides
RRNPPA family
Results reveal
Receptor specificity
Quorum sensing
qs communication
Produced pheromones
Processes governing
Pheromone duplication
Mediating communication
Intricate nature
Functional significance
Functional activities
Extracellular proteolysis
Extracellular proteases
Diversify peptide
Changing environments
Central role
Biological responses
Bacteriophages infecting
Bacterial interactions
Active pheromones
Quorum Sensing
Bacillus subtilis
https://www.ncbi.nlm.nih.gov/mesh/68053038
https://www.ncbi.nlm.nih.gov/mesh/68001412
topic Small signaling molecules
Produce identical structural
Opening new possibilities
Exhibit different types
Microbial social behaviors
Bacillus subtilis
Prevalent qs systems
Systems playing
Coordinating behaviors
Bacillota
Varying affinities
Several cases
Secreted oligopeptides
RRNPPA family
Results reveal
Receptor specificity
Quorum sensing
qs communication
Produced pheromones
Processes governing
Pheromone duplication
Mediating communication
Intricate nature
Functional significance
Functional activities
Extracellular proteolysis
Extracellular proteases
Diversify peptide
Changing environments
Central role
Biological responses
Bacteriophages infecting
Bacterial interactions
Active pheromones
Quorum Sensing
Bacillus subtilis
https://www.ncbi.nlm.nih.gov/mesh/68053038
https://www.ncbi.nlm.nih.gov/mesh/68001412
description (a) RMSD calculation from the superimposition of Cα atoms of Rap3T structures in complex with peptides SRGHTS, RGHTS, RRGHTA, and RRGHTAS. RMSD were calculated from individual monomers (lower) and dimers (upper). Number of atoms used in RMSD calculation is showed between parenthesis. (b) Superposition of 4 Rap3T-Peptide complexes with different pheromone variants in monomeric state RRGHTAS (blue), RRGHTA (pink), RGHTS (light green), and SRGHTS (orange). (c) Superposition of dimers for the 4 Rap3T complexes with peptides RRGHTAS (blue), RRGHTA (pink), RGHTS (light green), and SRGHTS (orange).
publishDate 2024
dc.date.none.fl_str_mv 2024
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/dataset
http://purl.org/coar/resource_type/c_ddb1
Publisher's version
info:eu-repo/semantics/publishedVersion
format dataset
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/372064
url http://hdl.handle.net/10261/372064
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Felipe-Ruiz, Alonso; Zamora-Caballero, Sara; Bendori, Shira Omer; Penadés, José R.; Eldar, Avigdor; Marina, Alberto (2024) Extracellular proteolysis of tandemly duplicated pheromone propeptides affords additional complexity to bacterial quorum sensing. PLoS - Biology 22(8):e3002744. https://doi.org/10.1371/journal.pbio.3002744. http://hdl.handle.net/10261/368076
https://doi.org/10.1371/journal.pbio.3002744.s004
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Figshare
publisher.none.fl_str_mv Figshare
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869425802065477632
score 15,811543

Registos relacionados