Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif

21 p.- 7 fig.- 4 tab.-2 fig. supl.-1 tab. supl.

Detalles Bibliográficos
Autores: Bustamante, Noemí, Campillo, Nuria E., García, Ernesto, Gallego-Páramo, Cristina, Pera, Benet, Diakun, Gregory P., Sáiz, José Luis, García González, Pedro, Díaz, José Fernando, Menéndez, Margarita
Tipo de recurso: artículo
Fecha de publicación:2010
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/52343
Acceso en línea:http://hdl.handle.net/10261/52343
Access Level:acceso abierto
Palabra clave:Bacteriophage
Biophysics
Circular dichroism
Computer modeling
Ultracentrifugation
CW-7 motif
Cpl-7 endolysin structure
SAXS
Streptococcus pneumoniae
Cell wall hydrolases
id ES_a94d5dc286ba3e06c4ee5b9089efdda7
oai_identifier_str oai:digital.csic.es:10261/52343
network_acronym_str ES
network_name_str España
repository_id_str
spelling Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding MotifBustamante, NoemíCampillo, Nuria E.García, ErnestoGallego-Páramo, CristinaPera, BenetDiakun, Gregory P.Sáiz, José LuisGarcía González, PedroDíaz, José FernandoMenéndez, MargaritaBacteriophageBiophysicsCircular dichroismComputer modelingUltracentrifugationCW-7 motifCpl-7 endolysin structureSAXSStreptococcus pneumoniaeCell wall hydrolases21 p.- 7 fig.- 4 tab.-2 fig. supl.-1 tab. supl.Bacteriophage endolysins include a group of new antibacterials reluctant to development of resistance. We present here the first structural study of the Cpl-7 endolysin, encoded by pneumococcal bacteriophage Cp-7. It contains an N-terminal catalytic module (CM) belonging to the GH25 family of glycosyl hydrolases and a C-terminal region encompassing three identical repeats of 42 amino acids (CW_7 repeats). These repeats are unrelated to choline-targeting motifs present in other cell wall hydrolases produced by Streptococcus pneumoniae and its bacteriophages, and are responsible for the protein attachment to the cell wall. By combining different biophysical techniques and molecular modeling, a three-dimensional model of the overall protein structure is proposed, consistent with circular dichroism and sequence-based secondary structure prediction, small angle x-ray scattering data, and Cpl-7 hydrodynamic behavior. Cpl-7 is an ∼115-Å long molecule with two well differentiated regions, corresponding to the CM and the cell wall binding region (CWBR), arranged in a lateral disposition. The CM displays the (βα)5β3 barrel topology characteristic of the GH25 family, and the impact of sequence differences with the CM of the Cpl-1 lysozyme in substrate binding is discussed. The CWBR is organized in three tandemly assembled three-helical bundles whose dispositions remind us of a super-helical structure. Its approximate dimensions are 60 × 20 × 20 Å and presents a concave face that might constitute the functional region involved in bacterial surface recognition. The distribution of CW_7 repeats in the sequences deposited in the Entrez Database have been examined, and the results drastically expanded the antimicrobial potential of the Cpl-7 endolysinThis work was supported by Grants BFU2006-10288, SAF2009-10824, BIO2007-61336, and BFU2009-10052 from Ministerio de Ciencia e Innovación, Grant BIPPED-CM from the Comunidad de Madrid, the CIBER de Enfermedades Respiratorias (CIBERES), an initiative of the ISCIII, Glycodynamics Network Grant FP6-UE MCTN-CT-2005-019561, and European Community beam time Proposal 48086Peer reviewedAmerican Society for Biochemistry and Molecular Biology2010info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/52343reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1074/jbc.M110.154559info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/523432026-05-22T06:33:51Z
dc.title.none.fl_str_mv Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
title Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
spellingShingle Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
Bustamante, Noemí
Bacteriophage
Biophysics
Circular dichroism
Computer modeling
Ultracentrifugation
CW-7 motif
Cpl-7 endolysin structure
SAXS
Streptococcus pneumoniae
Cell wall hydrolases
title_short Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
title_full Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
title_fullStr Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
title_full_unstemmed Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
title_sort Cpl-7, a Lysozyme Encoded by a Pneumococcal Bacteriophage with a Novel Cell Wall-Binding Motif
dc.creator.none.fl_str_mv Bustamante, Noemí
Campillo, Nuria E.
García, Ernesto
Gallego-Páramo, Cristina
Pera, Benet
Diakun, Gregory P.
Sáiz, José Luis
García González, Pedro
Díaz, José Fernando
Menéndez, Margarita
author Bustamante, Noemí
author_facet Bustamante, Noemí
Campillo, Nuria E.
García, Ernesto
Gallego-Páramo, Cristina
Pera, Benet
Diakun, Gregory P.
Sáiz, José Luis
García González, Pedro
Díaz, José Fernando
Menéndez, Margarita
author_role author
author2 Campillo, Nuria E.
García, Ernesto
Gallego-Páramo, Cristina
Pera, Benet
Diakun, Gregory P.
Sáiz, José Luis
García González, Pedro
Díaz, José Fernando
Menéndez, Margarita
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Bacteriophage
Biophysics
Circular dichroism
Computer modeling
Ultracentrifugation
CW-7 motif
Cpl-7 endolysin structure
SAXS
Streptococcus pneumoniae
Cell wall hydrolases
topic Bacteriophage
Biophysics
Circular dichroism
Computer modeling
Ultracentrifugation
CW-7 motif
Cpl-7 endolysin structure
SAXS
Streptococcus pneumoniae
Cell wall hydrolases
description 21 p.- 7 fig.- 4 tab.-2 fig. supl.-1 tab. supl.
publishDate 2010
dc.date.none.fl_str_mv 2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/52343
url http://hdl.handle.net/10261/52343
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1074/jbc.M110.154559
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869416009192964096
score 15,812429