3HF2

Crystal structure of the I401P mutant of cytochrome P450 BM3

Summary for 3HF2

• Entry DOI: 10.2210/pdb3hf2/pdb
• Descriptor: Bifunctional P-450/NADPH-P450 reductase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: p450 family protein fold, oxidoreductase, electron transport, fad, flavoprotein, fmn, heme, iron, metal-binding, monooxygenase, multifunctional enzyme, nadp, transport
• Biological source: Bacillus megaterium
• Cellular location: Cytoplasm (By similarity): P14779
• Total number of polymer chains: 2
• Total formula weight: 111244.26

Authors

Yang, W.,Whitehouse, C.J.C.,Bell, S.G.,Bartlam, M.,Wong, L.L.,Rao, Z. (deposition date: 2009-05-10, release date: 2009-06-30, Last modification date: 2023-11-01)

Primary citation

Whitehouse, C.J.C.,Bell, S.G.,Yang, W.,Yorke, J.A.,Blanford, C.F.,Strong, A.J.F.,Morse, E.J.,Bartlam, M.,Rao, Z.,Wong, L.-L.
A Highly Active Single-Mutation Variant of P450(BM3) (CYP102A1)
Chembiochem, 10:1654-1656, 2009

PubMed Abstract: The power of proline: Bold amino acid substitutions in sensitive protein regions are frequently unproductive, while more subtle mutations can be sufficient to bring about dramatic changes. But introducing proline at the residue next to the sulfur ligand in P450(BM3) (CYP102A1) has the unexpected and desirable effect of enhancing the activity of this fatty acid hydroxylase with a broad range of non-natural substrates, as illustrated by the figure.

PubMed: 19492389
DOI: 10.1002/cbic.200900279

Experimental method

X-RAY DIFFRACTION (2.2 Å)