Crystal structure of AliD in the open conformation [Dataset]
(A) Molecular surface and topology of AliD. The upper panel illustrates the molecular surface representation of AliD, with each domain color-coded. In the lower panel, a topological diagram depicts the secondary structure elements of AliD, labeled and numbered. The color code spans from blue (N-term...
| 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:10261/374359 |
| Acceso en línea: | http://hdl.handle.net/10261/374359 |
| 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) Molecular surface and topology of AliD. The upper panel illustrates the molecular surface representation of AliD, with each domain color-coded. In the lower panel, a topological diagram depicts the secondary structure elements of AliD, labeled and numbered. The color code spans from blue (N-terminus) to red (C-terminus), portraying α-helices as cylinders and β-strands as arrows. (B) Overall cartoon representation of AliD monomer structure. The structure is presented in two orientations spaced 180° apart. Domains I, II, and III are labeled and colored green, light orange, and blue, respectively. The dimensions of the peptide-binding cavity (~16 Å in width and ~45 Å in height) are specified. The C-terminal α-helix (α19) is highlighted in red and labeled. N, amino-terminus; C, Carboxy-terminus. |
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