Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/74336
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Homology modelling and active-site-mutagenesis study of the catalytic domain of the pneumococcal phosphorylcholine esterase |
Autor: | Campillo, Nuria E. CSIC ORCID ; Páez, Juan A. CSIC ORCID; Lagartera, Laura CSIC ORCID; González, A. | Fecha de publicación: | 2005 | Editor: | Elsevier | Citación: | Bioorganic and Medicinal Chemistry 13(23):6404-6413(2005) | Resumen: | Streptococcus pneumoniae is among the major human pathogens. Several interactions of this bacterium with its host appear to have been mediated by bacterial cell wall components. Specifically, phosphorylcholine residues covalently attached to teichoic and lipoteichoic acids serve as anchors for many surface-located proteins (choline-binding proteins CBPs), including cell-adhesion and virulence factors, and are also recognized by host response components through choline-binding receptors. In this study, we have performed modelling of the catalytic domain of pneumococcal phosphorylcholine esterase (Pce), a modular enzyme that is capable of removing phosphorycholine residues from teichoic and lipoteichoic acids, remodelling their distribution on the bacterial envelope. We wish to contribute to the structural knowledge of Pce. In this pursuit, 3D models of Pce have been established by homology modelling, using the X-ray structure of enzymes from the α/β metallo-lactamase family fold as templates. Theoretical models of pneumococcal phosphorylcholine esterase (Pce) catalytic modules obtained by homology modelling, and corresponding docking studies employed to find out the residues involved in the binding of Zn ions, are discussed according to mutational studies and ab initio calculations. The presence of a binuclear Zn cluster in the catalytic domain of Pce and a likely coordination model are proposed. © 2005 Elsevier Ltd. All rights reserved. | Versión del editor: | http://dx.doi.org/10.1016/j.bmc.2005.06.060 | URI: | http://hdl.handle.net/10261/74336 | DOI: | 10.1016/j.bmc.2005.06.060 | ISSN: | 0968-0896 | E-ISSN: | 1464-3391 |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
1
checked on 20-mar-2024
Page view(s)
387
checked on 26-mar-2024
Download(s)
101
checked on 26-mar-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.