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Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin

Bin Zhao, Suzy C. Moody, Robert C. Hider, Li Lei, Steven Kelly Orcid Logo, Michael R. Waterman, David C. Lamb

International Journal of Molecular Sciences, Volume: 13, Issue: 7, Pages: 8500 - 8513

Swansea University Author: Steven Kelly Orcid Logo

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DOI (Published version): 10.3390/ijms13078500

Abstract

Coelibactin is a putative non-ribosomally synthesized peptide with predicted zincophore activity and which has been implicated in antibiotic regulation in Streptomyces coelicolor A3(2). The coelibactin biosynthetic pathway contains a stereo- and regio-specific monooxygenation step catalyzed by a cyt...

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Published in: International Journal of Molecular Sciences
ISSN: 1422-0067
Published: MDPI AG 2012
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URI: https://cronfa.swan.ac.uk/Record/cronfa13027
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Abstract: Coelibactin is a putative non-ribosomally synthesized peptide with predicted zincophore activity and which has been implicated in antibiotic regulation in Streptomyces coelicolor A3(2). The coelibactin biosynthetic pathway contains a stereo- and regio-specific monooxygenation step catalyzed by a cytochrome P450 enzyme (CYP105N1). We have determined the X-ray crystal structure of CYP105N1 at 2.9 Å and analyzed it in the context of the bacterial CYP105 family as a whole. The crystal structure reveals a channel between the α-helical domain and the β-sheet domain exposing the heme pocket and the long helix I to the solvent. This wide-open conformation of CYP105N1 may be related to the bulky substrate coelibactin. The ligand-free CYP105N1 structure has enough room in the substrate access channel to allow the coelibactin to enter into the active site. Analysis of typical siderophore ligands suggests that CYP105N1 may produce derivatives of coelibactin, which would then be able to chelate the zinc divalent cation
College: Swansea University Medical School
Issue: 7
Start Page: 8500
End Page: 8513