The prokaryotic Cys2His2 zinc finger domain adopts a novel fold as revealed by the solution structure of Agrobacterium tumefaciens Ros DNA binding domain (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• The prokaryotic Cys2His2 zinc finger domain adopts a novel fold as revealed by the solution structure of Agrobacterium tumefaciens Ros DNA binding domain (Articolo in rivista) (literal)

Anno

• 2007-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1073/pnas.0706659104 (literal)

Alternative label

• G. Malgieri, L. Russo, S. Esposito, I. Baglivo, L. Zaccaro, E. M. Pedone, B. Di Blasio, C. Isernia, P. V. Pedone and R. Fattorusso (2007)
  The prokaryotic Cys2His2 zinc finger domain adopts a novel fold as revealed by the solution structure of Agrobacterium tumefaciens Ros DNA binding domain
  in Proceedings of the National Academy of Sciences of the United States of America
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• G. Malgieri, L. Russo, S. Esposito, I. Baglivo, L. Zaccaro, E. M. Pedone, B. Di Blasio, C. Isernia, P. V. Pedone and R. Fattorusso (literal)

Pagina inizio

• 17341 (literal)

Pagina fine

• 17346 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 104 (literal)

Rivista

• Proceedings of the National Academy of Sciences of the United States of America (Rivista)

Note

• Scopu (literal)
• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• *Dipartimento di Scienze Ambientali, Seconda Universita` degli Studi di Napoli, Via Vivaldi 43, 81100 Caserta, Italy; and +Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, 80134 Napoli, Italy (literal)

Titolo

• The prokaryotic Cys2His2 zinc finger domain adopts a novel fold as revealed by the solution structure of Agrobacterium tumefaciens Ros DNA binding domain (literal)

Abstract

• The first putative prokaryotic Cys2His2 zinc-finger domain has been identified in the transcriptional regulator Ros from Agrobacterium tumefaciens, indicating that the Cys2His2 zinc-finger domain, originally thought to be confined to the eukaryotic kingdom, could be widespread throughout the living kingdom from eukaryotic, both animal and plant, to prokaryotic. In this article we report the NMR solution structure of Ros DNA-binding domain (Ros87), providing 79 structural characterization of a prokaryotic Cys2His2 zinc-finger domain. The NMR structure of Ros87 shows that the putative prokaryotic Cys2His2 zinc-finger sequence is indeed part of a significantly larger zinc-binding globular domain that possesses a novel protein fold very different from the classical fold reported for the eukaryotic classical zinc-finger. The Ros87 globular domain consists of 58 aa (residues 9-66), is arranged in a ????? topology, and is stabilized by an extensive 15-residue hydrophobic core. A backbone dynamics study of Ros87, based on 15N R1, 15N R2, and heteronuclear 15N-{1H}-NOE measurements, has further confirmed that the globular domain is uniformly rigid and flanked by two flexible tails. Mapping of the amino acids necessary for the DNA binding onto Ros87 structure reveals the protein surface involved in the DNA recognition mechanism of this new zinc-binding protein domain. (literal)

Prodotto di

• Sviluppo di sistemi molecolari per il delivery di farmaci e diagnostici (PM.P01.003.003) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• EMILIA MARIA PEDONE (Unità di personale interno)
• LAURA ZACCARO (Persona)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Sviluppo di sistemi molecolari per il delivery di farmaci e diagnostici (PM.P01.003.003) (Modulo)

Autore CNR di

• EMILIA MARIA PEDONE (Unità di personale interno)
• LAURA ZACCARO (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Proceedings of the National Academy of Sciences of the United States of America (Rivista)