Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 528, Issue 2, Pages 111-117Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2012.09.001
Keywords
P450; CYP105N1; Streptomyces coelicolor; Coelibactin; Estradiol
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Funding
- National Research Foundation of Korea (NRF)
- Korea government (MEST) [2011-0016509]
- National Research Foundation of Korea [2011-0016509] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The genome sequence of Streptomyces coelicolor contains 18 cytochrome P450 enzymes. The recombinant CYP105N1 protein has been expressed in Escherichia coli and purified, and we report the biochemical and structural characterization of CYP105N1 from S. coelicolor. The purified protein exhibited the typical CO-binding spectrum of P450 enzymes and type I binding spectra with estradiol and a coelibactin analog. The oxidation of estradiol by CYP105N1, supported by H2O2, produced estriol. The crystal structure of CYP105N1 was determined at 2.9 angstrom resolution. An unexpected wide open binding pocket located above the heme group was identified, with a volume of approximately 4299 angstrom(3). These results suggest that the large open pocket to the active site may be a key feature for easy access of the peptidyl carrier protein-bound substrate to perform the hydroxylation reaction. A molecular docking model with coelibactin showed that the phenyl group of coelibactin is located <4 angstrom away from the heme-iron, suggesting that CYP105N1 may be involved in the hydroxylation of the phenyl ring of the coelibactin precursor during biosynthesis. (C) 2012 Elsevier Inc. All rights reserved.
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