5xnt

Structure of CYP106A2 from Bacillus sp. PAMC 23377

spinqualitylabelsall models 5xnt, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xnt is a 1 chain structure with sequence from Peribacillus butanolivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CPXM_PRIMG Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position. Publication Abstract from PubMed Bacterial cytochrome P450 (CYP) steroid hydroxylases are effectively useful in the pharmaceutical industry for introducing hydroxyl groups to a wide range of steroids. We found a putative CYP steroid hydroxylase (BaCYP106A2) from the bacterium Bacillus sp. PAMC 23377 isolated from Kara Sea of the Arctic Ocean, showing 94% sequence similarity with BmCYP106A2 (Bacillus megaterium ATCC 13368). In this study, soluble BaCYP106A2 was overexpressed to evaluate its substrate-binding activity. The substrate affinity (Kd value) to 4-androstenedione was 387 +/- 37 microM. Moreover, the crystal structure of BaCYP106A2 was determined at 2.7 A resolution. Structural analysis suggested that the alpha8-alpha9 loop region of BaCYP106A2 is intrinsically mobile and might be important for initial ligand binding. The hydroxyl activity of BaCYP106A2 was identified using in vitro enzyme assays. Its activity was confirmed with two kinds of steroid substrates, 4-androstenedione and nandrolone, using chromatography and mass spectrometry methods. The main products were monohydroxylated compounds with high conversion yields. This is the second study on the structure of CYP106A steroid hydroxylases, and should contribute new insight into the interactions of bacterial CYP106A with steroid substrates, providing baseline data for studying the CYP106A steroid hydroxylase from the structural and enzymatic perspectives. Crystal Structure and Functional Characterization of a Cytochrome P450 (BaCYP106A2) from Bacillus sp. PAMC 23377.,Kim KH, Lee CW, Dangi B, Park SH, Park H, Oh TJ, Lee JH J Microbiol Biotechnol. 2017 Aug 28;27(8):1472-1482. doi: 10.4014/jmb.1706.06013. PMID:28633515 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

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