Substrate trapped in AmiA during the purification process [Dataset]

(A) Ribbon representation of AmiA structure in complex with an unknown peptide from E. coli (in yellow caped sticks) that we further refined as peptide 4. (B) Electron-density map (2mFo-DFc map contoured at 1.0 σ) for the 10-residues long ligand has been traced (yellow caped sticks) assuming the seq...

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Detalles Bibliográficos
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:10261/374794
Acceso en línea:http://hdl.handle.net/10261/374794
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
Descripción
Sumario:(A) Ribbon representation of AmiA structure in complex with an unknown peptide from E. coli (in yellow caped sticks) that we further refined as peptide 4. (B) Electron-density map (2mFo-DFc map contoured at 1.0 σ) for the 10-residues long ligand has been traced (yellow caped sticks) assuming the sequence of peptide 4 (AKTIKITQTR). Ligand is presented in a similar orientation as the one found on panel A. Positions for each residue are indicated.

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