Journal article 1044 views
Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
,
Michael R. Waterman,
David C. Lamb
International Journal of Molecular Sciences, Volume: 13, Issue: 7, Pages: 8500 - 8513
Swansea University Author:
Steven Kelly
Full text not available from this repository: check for access using links below.
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...
| Published in: | International Journal of Molecular Sciences |
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| ISSN: | 1422-0067 |
| Published: |
MDPI AG
2012
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| Online Access: |
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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 |
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| College: |
Faculty of Medicine, Health and Life Sciences |
| Issue: |
7 |
| Start Page: |
8500 |
| End Page: |
8513 |