Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of C-12 hydroxylase EryK from Saccharopolyspora erythraea

Carmelinda, Savino; Sciara, Giuliano; Miele, Adriana Erica; Steven, Kendrew; Vallone, Beatrice

doi:10.2174/092986608786071201

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 P21 or to the orthorhombic P212121 space groups, and exhibit diffraction limits ranging from 2.3 to 1.6 Å. The structures will be determined by molecular replacement. © 2008 Bentham Science Publishers Ltd.

Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of C-12 hydroxylase EryK from Saccharopolyspora erythraea / Carmelinda, Savino; Sciara, Giuliano; Miele, Adriana Erica; Steven, Kendrew; Vallone, Beatrice. - In: PROTEIN AND PEPTIDE LETTERS. - ISSN 0929-8665. - 15:10(2008), pp. 1138-1141.

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Titolo:	Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of C-12 hydroxylase EryK from Saccharopolyspora erythraea
Autori:	Carmelinda Savino SCIARA, Giuliano MIELE, Adriana Erica Steven Kendrew VALLONE, Beatrice mostra contributor esterni nascondi contributor esterni
Data di pubblicazione:	2008
Rivista:	PROTEIN AND PEPTIDE LETTERS
Citazione:	Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of C-12 hydroxylase EryK from Saccharopolyspora erythraea / Carmelinda, Savino; Sciara, Giuliano; Miele, Adriana Erica; Steven, Kendrew; Vallone, Beatrice. - In: PROTEIN AND PEPTIDE LETTERS. - ISSN 0929-8665. - 15:10(2008), pp. 1138-1141.
Handle:	http://hdl.handle.net/11573/229185
Appartiene alla tipologia:	01a Articolo in rivista

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