Functional analysis and crystallographic structure of clotrimazole bound OleP, a cytochrome P450 epoxidase from Streptomyces antibioticus involved in oleandomycin biosynthesis
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- 作者：Linda Celeste Montemiglioa ; b ; 1 ; Giacomo Parisia ; b ; 1 ; Antonella Scaglionea ; b ; Giuliano Sciaraa ; b ; 2 ; Carmelinda Savinoc ; linda.savino@uniroma1.it" class="auth_mail" title="E-mail the corresponding author ; Beatrice Vallonea ; b ; c ; beatrice.vallone@uniroma1.it" class="auth_mail" title="E-mail the corresponding author
- 关键词：OleP ; 8.8a-deoxyoleandolide epoxigenase ; P450 ; cytochrome P450 ; EpoK ; Epothilone C&ndash ; D monooxygenase ; PimD ; Pimaricin monooxygenase ; MycG ; Mycinamicin monooxygenase ; CLT ; clotrimazole ; KC ; ketoconazole ; DMSO ; dimethyl sulfoxide ; DEO ; 8.8a-deoxyoleandolide ; LO-DEO ; L-olivosyl-8.8a-deoxyoleandolide ; CTZ&ndash ; OleP ; OleP in complex with CTZ ; rmsd ; root mean square deviation ; M-III ; mycinamicin III ; M-IV ; mycinamicin IV ; M-V ; mycinamicin V ; i.s. ; ionic strength ; SEC ; Size Exclusion Chromatograph
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：1860
- 期：3
- 页码：465-475
- 全文大小：1576 K
文摘
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Report of the structure of OleP P450 epoxidase acting on aliphatic carbons
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P450 epoxidase OleP binds clotrimazole following a simple one-step mechanism.
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In complex with clotrimazole OleP adopts an open conformation.
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Clotrimazole contacts residues involved in substrate recognition.