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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Agriculture / Faculty of Agriculture >
Peer-reviewed Journal Articles, etc >
Crystal structure of cytochrome P450 MoxA from Nonomuraea recticatena (CYP105)
| Title: | Crystal structure of cytochrome P450 MoxA from Nonomuraea recticatena (CYP105) |
| Authors: | Yasutake, Yoshiaki Browse this author | | Imoto, Noriko Browse this author | | Fujii, Yoshikazu Browse this author | | Fujii, Tadashi Browse this author | | Arisawa, Akira Browse this author | | Tamura, Tomohiro Browse this author →KAKEN DB |
| Keywords: | Crystal structure | | CYP105 | | Cytochrome P450 | | MoxA | | Nonomuraea recticatena |
| Issue Date: | 5-Oct-2007 |
| Publisher: | Elsevier Inc. |
| Journal Title: | Biochemical and Biophysical Research Communications |
| Volume: | 361 |
| Issue: | 4 |
| Start Page: | 876 |
| End Page: | 882 |
| Publisher DOI: | 10.1016/j.bbrc.2007.07.062 |
| PMID: | 17679139 |
| Abstract: | Cytochrome P450 MoxA (P450moxA) from a rare actinomycete Nonomuraea recticatena belongs to the CYP105 family and exhibits remarkably broad substrate specificity. Here, we demonstrate that P450moxA acts on several luciferin derivatives, which were originally identified as substrates of the human microsomal P450s. We also describe the crystal structure of P450moxA in substrate-free form. Structural comparison with various bacterial and human microsomal P450s reveals that the P450moxA structure is most closely related to that of the fungal nitric oxide reductase P450nor (CYP55A1). Final refined model of P450moxA comprises almost all the residues, including the “BC-loop” and “FG-loop” regions pivotal for substrate recognition, and the current structure thus defines a well-ordered substrate-binding pocket. Clear electron density map reveals that the MES molecule is bound to the substrate-binding site, and the sixth coordination position of the heme iron is not occupied by a water molecule, probably due to the presence of MES molecule in the vicinity of the heme. The unexpected binding of the MES molecule might reflect the ability of P450moxA to accommodate a broad range of structurally diverse compounds. |
| Relation: | http://www.sciencedirect.com/science/journal/0006291X |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/30116 |
| Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 田村 具博
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