Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/31393
COMPARTIR / EXPORTAR:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator

AutorGomis-Rüth, F. Xavier CSIC ORCID ; Solà, Maria CSIC ORCID ; Acebo País, Paloma CSIC; Párraga, Antonio CSIC; Guasch, Alicia CSIC ; Eritja Casadellà, Ramón CSIC ORCID ; González, Ana CSIC; Solar, Gloria del CSIC ORCID ; Coll, Miquel CSIC ORCID
Palabras claveCopG
Plasmids
Protein–DNA complex
Transcriptional repressor
X-ray crystal structure
Fecha de publicación15-dic-1998
EditorNature Publishing Group
CitaciónEMBO Journal 17(24): 7404-7415 (1998)
ResumenThe structure of the 45 amino acid transcriptional repressor, CopG, has been solved unliganded and bound to its target operator DNA. The protein, encoded by the promiscuous streptococcal plasmid pMV158, is involved in the control of plasmid copy number. The structure of this protein repressor, which is the shortest reported to date and the first isolated from a plasmid, has a homodimeric ribbon-helix-helix arrangement. It is the prototype for a family of homologous plasmid repressors. CopG cooperatively associates, completely protecting several turns on one face of the double helix in both directions from a 13-bp pseudosymmetric primary DNA recognition element. In the complex structure, one protein tetramer binds at one face of a 19-bp oligonucleotide, containing the pseudosymmetric element, with two beta-ribbons inserted into the major groove. The DNA is bent 60 degrees by compression of both major and minor grooves. The protein dimer displays topological similarity to Arc and MetJ repressors. Nevertheless, the functional tetramer has a unique structure with the two vicinal recognition ribbon elements at a short distance, thus inducing strong DNA bend. Further structural resemblance is found with helix-turn-helix regions of unrelated DNA-binding proteins. In contrast to these, however, the bihelical region of CopG has a role in oligomerization instead of DNA recognition. This observation unveils an evolutionary link between ribbon-helix-helix and helix-turn-helix proteins.
Descripción12 pages, 6 figures, 2 tables.-- PMID: 9857196 [PubMed].-- PMCID: PMC1171085.
Versión del editorhttp://dx.doi.org/10.1093/emboj/17.24.7404
URIhttp://hdl.handle.net/10261/31393
DOI10.1093/emboj/17.24.7404
ISSN0261-4189
E-ISSN1460-2075
Aparece en las colecciones: (IDAEA) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
plasmid-encoded_transcriptional_CopG_Gomis.pdf510,4 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

CORE Recommender

PubMed Central
Citations

62
checked on 02-mar-2024

SCOPUSTM   
Citations

137
checked on 14-mar-2024

WEB OF SCIENCETM
Citations

134
checked on 25-feb-2024

Page view(s)

357
checked on 18-mar-2024

Download(s)

215
checked on 18-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.