Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]

(A) The bound peptides visualized inside the binding cavity of OBPs belonging to the Ami permease reveal the extent of the unoccupied space. The cavity is shown as a gray semi-transparent surface, the peptide is shown in yellow capped stick, and the protein is not shown. AmiA:5, AmiA in complex with...

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Autores: Alcorlo, Martín, Abdullah, Mohammed R., Steil, Leif, Sotomayor, Francisco, López de Oro, Laura, Castro, Sonia de, Velázquez, Sonsoles, Kohler, Thomas P., Jiménez, Elisabet, Medina, Ana, Usón, Isabel, Keller, Lance E., Bradshaw, Jessica L., McDaniel, Larry S., Camarasa Rius, María José, Völker, Uwe, Hammerschmidt, Sven, Hermoso, Juan A.
Tipo de recurso: conjunto de datos
Estado:Versión publicada
Fecha de publicación:2024
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/374492
Acceso en línea:http://hdl.handle.net/10261/374492
Access Level:acceso abierto
Palabra clave:Unexpected remarkable promiscuity
Streptococcus pneumoniae </
Produced de novo
Multiple crystallographic structures
Escherichia coli </
Diverse peptide specificities
Closed conformations along
Certain amino acids
>, displaying affinity
Ensure sufficient uptake
Mass spectrometry analysis
div >< p
Orchestrating oligopeptide uptake
Four proteins building
Ami transporter system
Abc transporter channel
Pneumococci
Structural analysis
Oligopeptide recognition
Oligopeptide binding
Uptake mechanism
Wide range
Vivo implications
Transport systems
Substantial array
Structural basis
Silico modelling
Shedding light
Oligopeptides demonstrates
Invasive infections
Energy balance
Cellular cytoplasm
Cell surface
Binding cassette
Becomes indispensable
Auxotrophic nature
Abc transporters
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oai_identifier_str oai:digital.csic.es:10261/374492
network_acronym_str ES
network_name_str España
repository_id_str
spelling Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]Alcorlo, MartínAbdullah, Mohammed R.Steil, LeifSotomayor, FranciscoLópez de Oro, LauraCastro, Sonia deVelázquez, SonsolesKohler, Thomas P.Jiménez, ElisabetMedina, AnaUsón, IsabelKeller, Lance E.Bradshaw, Jessica L.McDaniel, Larry S.Camarasa Rius, María JoséVölker, UweHammerschmidt, SvenHermoso, Juan A.Unexpected remarkable promiscuityStreptococcus pneumoniae </Produced de novoMultiple crystallographic structuresEscherichia coli </Diverse peptide specificitiesClosed conformations alongCertain amino acids>, displaying affinityEnsure sufficient uptakeMass spectrometry analysisdiv >< pOrchestrating oligopeptide uptakeFour proteins buildingAmi transporter systemAbc transporter channelPneumococciStructural analysisOligopeptide recognitionOligopeptide bindingUptake mechanismWide rangeVivo implicationsTransport systemsSubstantial arrayStructural basisSilico modellingShedding lightOligopeptides demonstratesInvasive infectionsEnergy balanceCellular cytoplasmCell surfaceBinding cassetteBecomes indispensableAuxotrophic natureAbc transporters(A) The bound peptides visualized inside the binding cavity of OBPs belonging to the Ami permease reveal the extent of the unoccupied space. The cavity is shown as a gray semi-transparent surface, the peptide is shown in yellow capped stick, and the protein is not shown. AmiA:5, AmiA in complex with peptide 5; AliD:1, AliD in complex with peptide 1; AliB:2, AliB in complex with peptide 2; AmiB:3, AmiB in complex with peptide 3 and AmiB:4, AmiB in complex with peptide 4. (B) Comparison of the binding cavity volumes found on SBPs of the Ami permease, including the cavities of OppA from L. lactis [PDB 3DRF [30]], AppA from B. subtillis (PDB 1XOC [31]), OppA from S. typhimurium [PDB 1B4Z [26]], DppA [PDB 1DPE] and ProX from E. coli [PDB 1SW2 [33]], for comparative purposes. The volumes were calculated with the program POCASA v1.1 [34] using default parameters and a Probe Radius of 1 Å.Peer reviewedPublic Library of ScienceConsejo 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/publishedVersionimage/tiffhttp://hdl.handle.net/10261/374492reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésAlcorlo, Martín; Abdullah, Mohammed R.; Steil, Leif; Sotomayor, Francisco; López de Oro, Laura; Castro, Sonia de ; Velázquez, Sonsoles; Kohler, Thomas P.; Jiménez, Elisabet; Medina, Ana; Usón, Isabel; Keller, Lance E.; Bradshaw, Jessica L..; McDaniel, Larry S.; Camarasa Rius, María José; Völker, Uwe; Hammerschmidt, Sven; Hermoso, Juan A. Molecular and structural basis of oligopeptide recognition by the Ami transporter system in pneumococci. https://doi.org/10.1371/journal.ppat.1011883 . http://hdl.handle.net/10261/364789https://doi.org/10.1371/journal.ppat.1011883.s024Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3744922026-05-22T06:33:51Z
dc.title.none.fl_str_mv Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
title Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
spellingShingle Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
Alcorlo, Martín
Unexpected remarkable promiscuity
Streptococcus pneumoniae </
Produced de novo
Multiple crystallographic structures
Escherichia coli </
Diverse peptide specificities
Closed conformations along
Certain amino acids
>, displaying affinity
Ensure sufficient uptake
Mass spectrometry analysis
div >< p
Orchestrating oligopeptide uptake
Four proteins building
Ami transporter system
Abc transporter channel
Pneumococci
Structural analysis
Oligopeptide recognition
Oligopeptide binding
Uptake mechanism
Wide range
Vivo implications
Transport systems
Substantial array
Structural basis
Silico modelling
Shedding light
Oligopeptides demonstrates
Invasive infections
Energy balance
Cellular cytoplasm
Cell surface
Binding cassette
Becomes indispensable
Auxotrophic nature
Abc transporters
title_short Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
title_full Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
title_fullStr Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
title_full_unstemmed Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
title_sort Substrate-binding cavities in OBPs of the Ami system and comparison with related proteins [Dataset]
dc.creator.none.fl_str_mv Alcorlo, Martín
Abdullah, Mohammed R.
Steil, Leif
Sotomayor, Francisco
López de Oro, Laura
Castro, Sonia de
Velázquez, Sonsoles
Kohler, Thomas P.
Jiménez, Elisabet
Medina, Ana
Usón, Isabel
Keller, Lance E.
Bradshaw, Jessica L.
McDaniel, Larry S.
Camarasa Rius, María José
Völker, Uwe
Hammerschmidt, Sven
Hermoso, Juan A.
author Alcorlo, Martín
author_facet Alcorlo, Martín
Abdullah, Mohammed R.
Steil, Leif
Sotomayor, Francisco
López de Oro, Laura
Castro, Sonia de
Velázquez, Sonsoles
Kohler, Thomas P.
Jiménez, Elisabet
Medina, Ana
Usón, Isabel
Keller, Lance E.
Bradshaw, Jessica L.
McDaniel, Larry S.
Camarasa Rius, María José
Völker, Uwe
Hammerschmidt, Sven
Hermoso, Juan A.
author_role author
author2 Abdullah, Mohammed R.
Steil, Leif
Sotomayor, Francisco
López de Oro, Laura
Castro, Sonia de
Velázquez, Sonsoles
Kohler, Thomas P.
Jiménez, Elisabet
Medina, Ana
Usón, Isabel
Keller, Lance E.
Bradshaw, Jessica L.
McDaniel, Larry S.
Camarasa Rius, María José
Völker, Uwe
Hammerschmidt, Sven
Hermoso, Juan A.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Unexpected remarkable promiscuity
Streptococcus pneumoniae </
Produced de novo
Multiple crystallographic structures
Escherichia coli </
Diverse peptide specificities
Closed conformations along
Certain amino acids
>, displaying affinity
Ensure sufficient uptake
Mass spectrometry analysis
div >< p
Orchestrating oligopeptide uptake
Four proteins building
Ami transporter system
Abc transporter channel
Pneumococci
Structural analysis
Oligopeptide recognition
Oligopeptide binding
Uptake mechanism
Wide range
Vivo implications
Transport systems
Substantial array
Structural basis
Silico modelling
Shedding light
Oligopeptides demonstrates
Invasive infections
Energy balance
Cellular cytoplasm
Cell surface
Binding cassette
Becomes indispensable
Auxotrophic nature
Abc transporters
topic Unexpected remarkable promiscuity
Streptococcus pneumoniae </
Produced de novo
Multiple crystallographic structures
Escherichia coli </
Diverse peptide specificities
Closed conformations along
Certain amino acids
>, displaying affinity
Ensure sufficient uptake
Mass spectrometry analysis
div >< p
Orchestrating oligopeptide uptake
Four proteins building
Ami transporter system
Abc transporter channel
Pneumococci
Structural analysis
Oligopeptide recognition
Oligopeptide binding
Uptake mechanism
Wide range
Vivo implications
Transport systems
Substantial array
Structural basis
Silico modelling
Shedding light
Oligopeptides demonstrates
Invasive infections
Energy balance
Cellular cytoplasm
Cell surface
Binding cassette
Becomes indispensable
Auxotrophic nature
Abc transporters
description (A) The bound peptides visualized inside the binding cavity of OBPs belonging to the Ami permease reveal the extent of the unoccupied space. The cavity is shown as a gray semi-transparent surface, the peptide is shown in yellow capped stick, and the protein is not shown. AmiA:5, AmiA in complex with peptide 5; AliD:1, AliD in complex with peptide 1; AliB:2, AliB in complex with peptide 2; AmiB:3, AmiB in complex with peptide 3 and AmiB:4, AmiB in complex with peptide 4. (B) Comparison of the binding cavity volumes found on SBPs of the Ami permease, including the cavities of OppA from L. lactis [PDB 3DRF [30]], AppA from B. subtillis (PDB 1XOC [31]), OppA from S. typhimurium [PDB 1B4Z [26]], DppA [PDB 1DPE] and ProX from E. coli [PDB 1SW2 [33]], for comparative purposes. The volumes were calculated with the program POCASA v1.1 [34] using default parameters and a Probe Radius of 1 Å.
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/10261/374492
url http://hdl.handle.net/10261/374492
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Alcorlo, Martín; Abdullah, Mohammed R.; Steil, Leif; Sotomayor, Francisco; López de Oro, Laura; Castro, Sonia de ; Velázquez, Sonsoles; Kohler, Thomas P.; Jiménez, Elisabet; Medina, Ana; Usón, Isabel; Keller, Lance E.; Bradshaw, Jessica L..; McDaniel, Larry S.; Camarasa Rius, María José; Völker, Uwe; Hammerschmidt, Sven; Hermoso, Juan A. Molecular and structural basis of oligopeptide recognition by the Ami transporter system in pneumococci. https://doi.org/10.1371/journal.ppat.1011883 . http://hdl.handle.net/10261/364789
https://doi.org/10.1371/journal.ppat.1011883.s024

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv image/tiff
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
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
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