The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis (Articolo in rivista)

Type
Label
  • The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1093/emboj/cdg031 (literal)
Alternative label
  • Sciara, G; Kendrew, SG; Miele, AE; Marsh, NG; Federici, L; Malatesta, F; Schimperna, G; Savino, C; Vallone, B (2003)
    The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis
    in EMBO journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Sciara, G; Kendrew, SG; Miele, AE; Marsh, NG; Federici, L; Malatesta, F; Schimperna, G; Savino, C; Vallone, B (literal)
Pagina inizio
  • 205 (literal)
Pagina fine
  • 215 (literal)
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  • 22 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • [1 ] Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy [ 2 ] Univ Roma La Sapienza, CNR, Ctr Studi Biol Mol, I-00185 Rome, Italy [ 3 ] Univ Aquila, Dipartimento Biol Base Applicata, I-67100 Laquila, Italy [ 4 ] Ist G Donegani SpA Montedison, I-28100 Novara, Italy [ 5 ] Biot Technol Ltd, Cambridge CB3 0DJ, England [ 6 ] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA (literal)
Titolo
  • The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis (literal)
Abstract
  • ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway is a member of a class of small monooxygenases that carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The overall structure is a ferredoxin-like fold with a novel, dimeric assembly, indicating that the widely represented ferredoxin fold may sustain yet another functionality. The resolution (1.3 Angstrom) of the enzyme structure and its complex with substrate and product analogues allows us to visualize the mechanism of binding and activation of the substrate for attack by molecular oxygen, and utilization of two gates for the reaction components including a proton gate and an O-2/H2O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure. (literal)
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