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Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin. / B Zhao; SC Moody; RC Hider; L Lei; Steven Kelly; MR Waterman; DC Lamb

Int J Mol Sci. 2012;13(7):8500-13., Volume: 13, Pages: 8500 - 8513

Swansea University Author: Steven, Kelly

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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: Int J Mol Sci. 2012;13(7):8500-13.
Published: 2012
URI: https://cronfa.swan.ac.uk/Record/cronfa13027
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spelling 2011-10-01T00:00:00.0000000 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 Int J Mol Sci. 2012;13(7):8500-13. 13 8500 8513 31 12 2012 2012-12-31 10.3390/ijms13078500 COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2011-10-01T00:00:00.0000000 2012-10-10T10:28:25.7305899 Swansea University Medical School Medicine B Zhao 1 SC Moody 2 RC Hider 3 L Lei 4 Steven Kelly 0000-0001-7991-5040 5 MR Waterman 6 DC 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 B Zhao
SC Moody
RC Hider
L Lei
Steven Kelly
MR Waterman
DC Lamb
format Journal article
container_title Int J Mol Sci. 2012;13(7):8500-13.
container_volume 13
container_start_page 8500
publishDate 2012
institution Swansea University
doi_str_mv 10.3390/ijms13078500
college_str Swansea University Medical School
hierarchytype
hierarchy_top_id swanseauniversitymedicalschool
hierarchy_top_title Swansea University Medical School
hierarchy_parent_id swanseauniversitymedicalschool
hierarchy_parent_title Swansea University Medical School
department_str Medicine{{{_:::_}}}Swansea University Medical School{{{_:::_}}}Medicine
document_store_str 0
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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 2012-12-31T03:25:46Z
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score 10.7876