2z36
From Proteopedia
(New page: 200px<br /><applet load="2z36" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z36, resolution 2.8Å" /> '''Crystal structure of ...) |
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==Overview== | ==Overview== | ||
| - | Cytochrome P450 MoxA (P450moxA) from a rare actinomycete Nonomuraea | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: p450]] | [[Category: p450]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:59:46 2008'' |
Revision as of 16:59, 21 February 2008
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Crystal structure of cytochrome P450 MoxA from Nonomuraea recticatena (CYP105)
Overview
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.
About this Structure
2Z36 is a Single protein structure of sequence from Nonomuraea recticatena with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of cytochrome P450 MoxA from Nonomuraea recticatena (CYP105)., Yasutake Y, Imoto N, Fujii Y, Fujii T, Arisawa A, Tamura T, Biochem Biophys Res Commun. 2007 Oct 5;361(4):876-82. Epub 2007 Jul 25. PMID:17679139
Page seeded by OCA on Thu Feb 21 18:59:46 2008
Categories: Nonomuraea recticatena | Single protein | Arisawa, A. | Fujii, T. | Fujii, Y. | Tamura, T. | Yasutake, Y. | FE | HEM | MES | Cyp105 | Oxidoreductase | P450
