Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/162271
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan |
Autor: | Bustamante, Noemí CSIC; Iglesias-Bexiga, Manuel CSIC; Bernardo-García, Noelia CSIC; Silva-Martín, Noella CSIC; García, Guadalupe CSIC; Campanero-Rhodes, María Asunción CSIC ORCID; García, Ernesto CSIC ORCID ; Usón, Isabel CSIC ORCID ; Martínez Buey, Rubén CSIC ORCID; García, Pedro CSIC ORCID ; Hermoso, Juan A. CSIC ORCID; Bruix, M. CSIC ORCID ; Menéndez, Margarita CSIC ORCID | Fecha de publicación: | 2017 | Editor: | Nature Publishing Group | Citación: | Scientific Reports 7 (2017) | Resumen: | Endolysins, the cell wall lytic enzymes encoded by bacteriophages to release the phage progeny, are among the top alternatives to fight against multiresistant pathogenic bacteria; one of the current biggest challenges to global health. Their narrow range of susceptible bacteria relies, primarily, on targeting specific cell-wall receptors through specialized modules. The cell wall-binding domain of Cpl-7 endolysin, made of three CW-7 repeats, accounts for its extended-range of substrates. Using as model system the cell wall-binding domain of Cpl-7, here we describe the molecular basis for the bacterial cell wall recognition by the CW-7 motif, which is widely represented in sequences of cell wall hydrolases. We report the crystal and solution structure of the full-length domain, identify N-acetyl-D-glucosaminyl-(β1,4)-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP) as the peptidoglycan (PG) target recognized by the CW-7 motifs, and characterize feasible GMDP-CW-7 contacts. Our data suggest that Cpl-7 cell wall-binding domain might simultaneously bind to three PG chains, and also highlight the potential use of CW-7-containing lysins as novel anti-infectives. | URI: | http://hdl.handle.net/10261/162271 | DOI: | 10.1038/s41598-017-16392-4 | Identificadores: | doi: 10.1038/s41598-017-16392-4 issn: 2045-2322 |
Aparece en las colecciones: | (IQF) Artículos (IBMB) Artículos (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
41598_2017_Article_16392.pdf | 4,19 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
11
checked on 24-mar-2024
SCOPUSTM
Citations
21
checked on 28-mar-2024
WEB OF SCIENCETM
Citations
21
checked on 28-feb-2024
Page view(s)
436
checked on 28-mar-2024
Download(s)
211
checked on 28-mar-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.