Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus

© 2014 IUBMB Life, 66(8):572-577, 2014 © 2014 International Union of Biochemistry and Molecular Biology. High-level resistance to β-lactam antibiotics in methicillin-resistant Staphylococcus aureus (MRSA) is due to expression of penicillin-binding protein 2a (PBP2a), a transpeptidase that catalyzes...

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Detalles Bibliográficos
Autores: Fishovitz, J., Hermoso, Juan A., Chang, M., Mobashery, S.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/167797
Acceso en línea:http://hdl.handle.net/10261/167797
Access Level:acceso abierto
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spelling Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureusFishovitz, J.Hermoso, Juan A.Chang, M.Mobashery, S.© 2014 IUBMB Life, 66(8):572-577, 2014 © 2014 International Union of Biochemistry and Molecular Biology. High-level resistance to β-lactam antibiotics in methicillin-resistant Staphylococcus aureus (MRSA) is due to expression of penicillin-binding protein 2a (PBP2a), a transpeptidase that catalyzes cell-wall crosslinking in the face of the challenge by β-lactam antibiotics. The activity of this protein is regulated by allostery at a site 60 Å distant from the active site, where crosslinking of cell wall takes place. This review discusses the state of knowledge on this important enzyme of cell-wall biosynthesis in MRSA.Peer ReviewedTaylor & FrancisConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2018201820142018info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/167797reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1677972026-05-22T06:33:51Z
dc.title.none.fl_str_mv Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
title Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
spellingShingle Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
Fishovitz, J.
title_short Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
title_full Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
title_fullStr Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
title_full_unstemmed Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
title_sort Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
dc.creator.none.fl_str_mv Fishovitz, J.
Hermoso, Juan A.
Chang, M.
Mobashery, S.
author Fishovitz, J.
author_facet Fishovitz, J.
Hermoso, Juan A.
Chang, M.
Mobashery, S.
author_role author
author2 Hermoso, Juan A.
Chang, M.
Mobashery, S.
author2_role author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description © 2014 IUBMB Life, 66(8):572-577, 2014 © 2014 International Union of Biochemistry and Molecular Biology. High-level resistance to β-lactam antibiotics in methicillin-resistant Staphylococcus aureus (MRSA) is due to expression of penicillin-binding protein 2a (PBP2a), a transpeptidase that catalyzes cell-wall crosslinking in the face of the challenge by β-lactam antibiotics. The activity of this protein is regulated by allostery at a site 60 Å distant from the active site, where crosslinking of cell wall takes place. This review discusses the state of knowledge on this important enzyme of cell-wall biosynthesis in MRSA.
publishDate 2014
dc.date.none.fl_str_mv 2014
2018
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/167797
url http://hdl.handle.net/10261/167797
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
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
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