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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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spelling 2021-10-29T09:48:50.7876428 v2 13027 2012-10-10 Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin b17cebaf09b4d737b9378a3581e3de93 0000-0001-7991-5040 Steven Kelly Steven Kelly true false 2012-10-10 BMS 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 Journal Article International Journal of Molecular Sciences 13 7 8500 8513 MDPI AG 1422-0067 31 12 2012 2012-12-31 10.3390/ijms13078500 http://dx.doi.org/10.3390/ijms13078500 COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2021-10-29T09:48:50.7876428 2012-10-10T10:28:25.7305899 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Bin Zhao 1 Suzy C. Moody 2 Robert C. Hider 3 Li Lei 4 Steven Kelly 0000-0001-7991-5040 5 Michael R. Waterman 6 David C. Lamb 7
title Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
spellingShingle Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
Steven Kelly
title_short Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
title_full Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
title_fullStr Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
title_full_unstemmed Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
title_sort Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
author_id_str_mv b17cebaf09b4d737b9378a3581e3de93
author_id_fullname_str_mv b17cebaf09b4d737b9378a3581e3de93_***_Steven Kelly
author Steven Kelly
author2 Bin Zhao
Suzy C. Moody
Robert C. Hider
Li Lei
Steven Kelly
Michael R. Waterman
David C. Lamb
format Journal article
container_title International Journal of Molecular Sciences
container_volume 13
container_issue 7
container_start_page 8500
publishDate 2012
institution Swansea University
issn 1422-0067
doi_str_mv 10.3390/ijms13078500
publisher MDPI AG
college_str Faculty of Medicine, Health and Life Sciences
hierarchytype
hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine
url http://dx.doi.org/10.3390/ijms13078500
document_store_str 0
active_str 0
description 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
published_date 2012-12-31T03:14:55Z
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score 11.013148

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