Structural basis for the properties of two single-site proline mutants of CYP102A1 (P450BM3).

Journal article

The crystal structures of the haem domains of Ala330Pro and Ile401Pro, two single-site proline variants of CYP102A1 (P450(BM3)) from Bacillus megaterium, have been solved. In the A330P structure, the active site is constricted by the relocation of the Pro329 side chain into the substrate access channel, providing a basis for the distinctive C-H bond oxidation profiles given by the variant and the enhanced activity with small molecules. I401P, which is exceptionally active towards non-natural ...

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Authors: Whitehouse, C; Yang, W; Yorke, J; Rowlatt, B; Strong, A

• Publication status: Published
• Journal: Chembiochem : a European journal of chemical biology
• Volume: 11
• Issue: 18
• Pages: 2549-2556
• Publication date: 2010-12-01
• DOI: 10.1002/cbic.201000421
• EISSN: 1439-7633
• ISSN: 1439-4227
• Language: English
• Keywords: Crystallography, X-Ray; Oxidation-Reduction; Substrate Specificity; Proline; Bacterial Proteins; NADPH-Ferrihemoprotein Reductase; Cytochrome P-450 Enzyme System; Bacillus megaterium; Electron Transport; Mutagenesis, Site-Directed; Protein Conformation; Models, Molecular