Structural and sequence comparison of AliD and OppA from S. typhimurium [Dataset]
(A) Left panel; superposition of the structures of AliD from S. pneumoniae (this work, colored in red) and OppA from S. typhimurium [colored in gray, PDB 1RKM [25]], both in the open conformation (rmsd of 3.18 Å for 349 Cα atoms). Right panel; structure superposition between AliD from S. pneumoniae...
| 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:10261/374846 |
| Acceso en línea: | http://hdl.handle.net/10261/374846 |
| 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 |
| Sumario: | (A) Left panel; superposition of the structures of AliD from S. pneumoniae (this work, colored in red) and OppA from S. typhimurium [colored in gray, PDB 1RKM [25]], both in the open conformation (rmsd of 3.18 Å for 349 Cα atoms). Right panel; structure superposition between AliD from S. pneumoniae (this work, colored in red) and OppA from S. typhimurium [colored in gray, PDB 1B4Z [26]], both in the closed conformation (rmsd of 3.20 Å for 347 Cα atoms). Both proteins are represented as cartoon oval. The two crossover connecting regions in AliD are colored yellow and labeled as "c1" and "c2", respectively. (B) Sequence alignment of AliD from S. pneumoniae and OppA from S. typhimurium, generated by T-COFFEE [22] and drawn with ESPript [23]. Sequence identity, estimated with Clustal2.1, is 25,76%. Identities are boxed in black. Similarities are boxed in gray according to physicochemical properties. |
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