Cloning, epression, purification, crystallization and preliminary X-ray crystallographic analyis of C-12 Hydroxylase EryK from Saccharoplyspora erythraea (Articolo in rivista)

Type
Label
  • Cloning, epression, purification, crystallization and preliminary X-ray crystallographic analyis of C-12 Hydroxylase EryK from Saccharoplyspora erythraea (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.2174/092986608786071201 (literal)
Alternative label
  • Savino,C.; Miele,A.E.; Sciara,G.; Kendrew,S.G.; Vallone,B. (2008)
    Cloning, epression, purification, crystallization and preliminary X-ray crystallographic analyis of C-12 Hydroxylase EryK from Saccharoplyspora erythraea
    in Protein and peptide letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Savino,C.; Miele,A.E.; Sciara,G.; Kendrew,S.G.; Vallone,B. (literal)
Pagina inizio
  • 1138 (literal)
Pagina fine
  • 1141 (literal)
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  • 15 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 4 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 10 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Univ Roma La Sapienza, Ist Biol & Patol Mol, CNR, I-00185 Rome, Italy 2. Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy 3. Biot Technol Ltd, Saffron Walden CB10 1XL, Essex, England (literal)
Titolo
  • Cloning, epression, purification, crystallization and preliminary X-ray crystallographic analyis of C-12 Hydroxylase EryK from Saccharoplyspora erythraea (literal)
Abstract
  • Erythromycin A is produced by Saccharopolyspora erythraea via a secondary metabolic pathway using several steps including glycosylations and hydroxylations of the first macrolide intermediate 6-deoxyerythronolide B. Erythromycin C-12 hydroxylase (CYP113A1), the P450 cytochrome active in the final stages of erythromycin biosynthesis, was cloned and expressed in E. coli. Different crystal forms were harvested from distinct crystallization conditions: two ligand-free forms, one substrate bound and two inhibitors-bound. All crystals belong either to the monoclinc P2(1) or to the orthorhombic P2(1)2(1)2(1) space groups, and exhibit diffraction limits ranging from 2.3 to 1.6 angstrom. The structures will be determined by molecular replacement. (literal)
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