Crystal structure of wild-type chaperonin GroEL (Articolo in rivista)

Type

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

Label

• Crystal structure of wild-type chaperonin GroEL (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Bartolucci C., Lamba D., Grazulis S., Manakova E., Heumann H. (2005)
  Crystal structure of wild-type chaperonin GroEL
  in Journal of Molecular Biology
  (literal)

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

• Bartolucci C., Lamba D., Grazulis S., Manakova E., Heumann H. (literal)

Pagina inizio

• 940 (literal)

Pagina fine

• 951 (literal)

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• 354 (literal)

Rivista

• Journal of Molecular Biology (Rivista)

Note

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

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

• Bartolucci C. -IC-CNR, Roma Lamba D. -IC-CNR, Trieste Grazulis S. -Institute of Biotechnology, Vilnius, Lithuania Manakova E. -Institute of Biotechnology, Vilnius, Lithuania Heumann H. -Max-Planck Institut für Biochemie, Martinsried bei München, Germany (literal)

Titolo

• Crystal structure of wild-type chaperonin GroEL (literal)

Abstract

• The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed in GroEL variants. Until now the crystal structure of the mutant Arg13Gly, Ala126Val GroEL was used for this purpose. We show that, due to the mutations as well as to the presence of a crystallographic symmetry, the ring-ring interface was inaccurately described. Analysis of the present structure allowed the definition of structural elements at this interface, essential for understanding the inter-ring allosteric signal transmission. We also show unambiguously that there is no ATP-induced 102 degrees rotation of the apical domain helix I around its helical axis, as previously assumed in the crystal structure of the (GroEL-KMgATP)(14) complex, and analyze the apical domain movements. These results enabled us to compare our structure with other GroEL crystal structures already published, allowing us to suggest a new route through which the allosteric signal for negative cooperativity propagates within the molecule. The proposed mechanism, supported by known mutagenesis data, underlines the importance of the switching of salt bridges. (literal)

Prodotto di

• Institute of Crystallography (IC) (Istituto)
• Studi strutturali e funzionali di proteine di interesse biomedico e biotecnologico (PM.P01.023.001) (Modulo)

Autore CNR

• DORIANO LAMBA (Unità di personale interno)
• CECILIA BARTOLUCCI (Unità di personale interno)

Incoming links:

Prodotto

• Institute of Crystallography (IC) (Istituto)
• Studi strutturali e funzionali di proteine di interesse biomedico e biotecnologico (PM.P01.023.001) (Modulo)

Autore CNR di

• DORIANO LAMBA (Unità di personale interno)
• CECILIA BARTOLUCCI (Unità di personale interno)

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

• Journal of Molecular Biology (Rivista)