Substrate recognition in AliD, AliB and AmiA [Dataset]
(A) Crystal structure of the AliD:peptide 1 complex. Left, ribbon representation of the AliD:peptide 1 complex (ligand shown in yellow caped sticks). Domains I, II, and III are labeled and colored green, light orange and blue; respectively. Right, a magnified view (corresponding to the boxed area sh...
| Autores: | , , , , , , , , , , , , , , , , , |
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| 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:10261/374351 |
| Acceso en línea: | http://hdl.handle.net/10261/374351 |
| 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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Substrate recognition in AliD, AliB and AmiA [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) Crystal structure of the AliD:peptide 1 complex. Left, ribbon representation of the AliD:peptide 1 complex (ligand shown in yellow caped sticks). Domains I, II, and III are labeled and colored green, light orange and blue; respectively. Right, a magnified view (corresponding to the boxed area shown in the left panel) highlighting amino acid residues engaged in the recognition of peptide 1 by AliD. Polar interactions are indicated by dotted black lines. The sequence of peptide 1 (FPPQNV) is illustrated in yellow capital letters. (B) The crystal structure of AliB in complex with peptides 2, 3 and 4. AliB, as observed in the AliB:peptide 2 complex, is depicted as a white cartoon. The substrates are represented with their secondary structure elements and are color-coded as yellow (peptide 2), green (peptide 3) and blue (peptide 4). (C) Stereo view illustrating polar interactions between AliB (white sticks) and peptide 2 (yellow sticks). (D) Stereo view showcasing polar interactions between AliB (white sticks) and peptide 3 (green sticks). (E) Stereo view illustrating polar interactions between AliB (white sticks) and peptide 4 (blue sticks). (F) Ribbon representation of AmiA in complex with peptide 4 (depicted as yellow capped sticks). (G) Stereo view providing specific details of peptide 4 recognition by AmiA. The relevant residues and crystallographic water molecules are depicted as gray-capped sticks and red spheres, respectively. Residues participating in hydrophobic interactions have been omitted for clarity. P1 to P6, pocket 1 to pocket 6. Pockets beyond substrate position 6 have been omitted for clarity.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/10261/374351reponame: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.g003Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3743512026-05-22T06:33:51Z |
| dc.title.none.fl_str_mv |
Substrate recognition in AliD, AliB and AmiA [Dataset] |
| title |
Substrate recognition in AliD, AliB and AmiA [Dataset] |
| spellingShingle |
Substrate recognition in AliD, AliB and AmiA [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 recognition in AliD, AliB and AmiA [Dataset] |
| title_full |
Substrate recognition in AliD, AliB and AmiA [Dataset] |
| title_fullStr |
Substrate recognition in AliD, AliB and AmiA [Dataset] |
| title_full_unstemmed |
Substrate recognition in AliD, AliB and AmiA [Dataset] |
| title_sort |
Substrate recognition in AliD, AliB and AmiA [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) Crystal structure of the AliD:peptide 1 complex. Left, ribbon representation of the AliD:peptide 1 complex (ligand shown in yellow caped sticks). Domains I, II, and III are labeled and colored green, light orange and blue; respectively. Right, a magnified view (corresponding to the boxed area shown in the left panel) highlighting amino acid residues engaged in the recognition of peptide 1 by AliD. Polar interactions are indicated by dotted black lines. The sequence of peptide 1 (FPPQNV) is illustrated in yellow capital letters. (B) The crystal structure of AliB in complex with peptides 2, 3 and 4. AliB, as observed in the AliB:peptide 2 complex, is depicted as a white cartoon. The substrates are represented with their secondary structure elements and are color-coded as yellow (peptide 2), green (peptide 3) and blue (peptide 4). (C) Stereo view illustrating polar interactions between AliB (white sticks) and peptide 2 (yellow sticks). (D) Stereo view showcasing polar interactions between AliB (white sticks) and peptide 3 (green sticks). (E) Stereo view illustrating polar interactions between AliB (white sticks) and peptide 4 (blue sticks). (F) Ribbon representation of AmiA in complex with peptide 4 (depicted as yellow capped sticks). (G) Stereo view providing specific details of peptide 4 recognition by AmiA. The relevant residues and crystallographic water molecules are depicted as gray-capped sticks and red spheres, respectively. Residues participating in hydrophobic interactions have been omitted for clarity. P1 to P6, pocket 1 to pocket 6. Pockets beyond substrate position 6 have been omitted for clarity. |
| 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 |
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dataset |
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publishedVersion |
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http://hdl.handle.net/10261/374351 |
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http://hdl.handle.net/10261/374351 |
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Inglés |
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Inglés |
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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.g003 Sí |
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openAccess |
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Public Library of Science |
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Public Library of Science |
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reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC instname:Consejo Superior de Investigaciones Científicas (CSIC) |
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Consejo Superior de Investigaciones Científicas (CSIC) |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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