Structure elucidation and 3D solution conformation of the antibiotic enduracidin determined by NMR spectroscopy and molecular dynamics (Articolo in rivista)

Type

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

Label

• Structure elucidation and 3D solution conformation of the antibiotic enduracidin determined by NMR spectroscopy and molecular dynamics (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Castiglione F., Marazzi A., Meli M., Colombo G. (2005)
  Structure elucidation and 3D solution conformation of the antibiotic enduracidin determined by NMR spectroscopy and molecular dynamics
  in Magnetic resonance in chemistry (Print)
  (literal)

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

• Castiglione F., Marazzi A., Meli M., Colombo G. (literal)

Pagina inizio

• 603 (literal)

Pagina fine

• 610 (literal)

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

• 43 (literal)

Rivista

• Magnetic resonance in chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Structure elucidation and 3D solution conformation of the antibiotic enduracidin determined by NMR spectroscopy and molecular dynamics (literal)

Abstract

• Enduracidin and ramoplanin belong to the large family of cyclodepsipeptide antibiotics, highly effective against Gram-positive bacteria. The primary and 3D solution structure of ramoplanin is already well known, and the primary structure of enduracidin has been determined by a combination of chemical and NMR spectroscopic methods. Both antibiotics share a similar peptide core of 17 amino acids and differ mainly in the length of the acyl chain and the presence of two D-mannose moieties in ramoplanin. Based on the high sequence homology with ramoplanin, the structure in solution of enduracidin is modeled as a cyclic peptide. The, tertiary structure thus obtained was refined. through molecular dynamics (MD) simulation, in which the interatomic NOE-derived distance restraints were imposed. MD simulations yielded a family of representative 3D structures (RMSD = 0.89), which highlighted a backbone geometry similar to that of ramoplanin in its beta-hairpin arrangement. In contrast, enduracidin displays a different arrangement of the side-chain and of the residues forming the hydrophobic core. (literal)

Prodotto di

• Modellistica molecolare di proteine legate a processi patologici (PM.P01.026.002) (Modulo)
• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)

Autore CNR

• MASSIMILIANO MELI (Unità di personale esterno)
• GIORGIO COLOMBO (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• Modellistica molecolare di proteine legate a processi patologici (PM.P01.026.002) (Modulo)

Autore CNR di

• GIORGIO COLOMBO (Unità di personale interno)
• MASSIMILIANO MELI (Unità di personale esterno)

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

• Magnetic resonance in chemistry (Rivista)