The antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus: an intrinsically stable cage-like structure endowed with enhanced stability (Articolo in rivista)

Type

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

Label

• The antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus: an intrinsically stable cage-like structure endowed with enhanced stability (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

Alternative label

• Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A (2006)
  The antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus: an intrinsically stable cage-like structure endowed with enhanced stability
  in The FEBS journal (Print)
  (literal)

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

• Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A (literal)

Pagina inizio

• 4913 (literal)

Pagina fine

• 4928 (literal)

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

• 273 (literal)

Rivista

• ?The ?FEBS journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• 1. Univ Roma La Sapienza, CNR, Ist Biol & Patol Mol, Dipartimento Sci Biochim, I-00185 Rome, Italy (literal)

Titolo

• The antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus: an intrinsically stable cage-like structure endowed with enhanced stability (literal)

Abstract

• Abstract: DNA-binding proteins from starved cells (Dps proteins) protect bacteria primarily from oxidative damage. They are composed of 12 identical subunits assembled with 23-symmetry to form a compact cage-like structure known to be stable at temperatures > 70 degrees C and over a wide pH range. Thermosynechococcus elongatus Dps thermostability is increased dramatically relative to mesophilic Dps proteins. Hydrophobic interactions at the dimeric and trimeric interfaces called Dps-like are replaced by salt bridges and hydrogen bonds, a common strategy in thermophiles. Moreover, the buried surface area at the least-extended Dps-like interface is significantly increased. A peculiarity of T. elongatus Dps is the presence of a chloride ion coordinated with threefold symmetry-related arginine residues lining the opening of the Dps-like pore toward the internal cavity. T. elongatus Dps conserves the unusual intersubunit ferroxidase centre that allows the Dps protein family to oxidize Fe(II) with hydrogen peroxide, thereby inhibiting free radical production via Fenton chemistry. This catalytic property is of special importance in T. elongatus (which lacks the catalase gene) in the protection of DNA and photosystems I and II from hydrogen peroxide-mediated oxidative damage. (literal)

Prodotto di

• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)
• Institute of molecular biology and pathology (IBPM) (Istituto)

Autore CNR

• ANDREA ILARI (Unità di personale interno)
• EMILIA CHIANCONE (Unità di personale esterno)
• PIERPAOLO CECI (Persona)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR di

• EMILIA CHIANCONE (Unità di personale esterno)
• ANDREA ILARI (Unità di personale interno)
• PIERPAOLO CECI (Persona)

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

• ?The ?FEBS journal (Rivista)