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Chembiochem. 2016 May 3;17(9):852-60. doi: 10.1002/cbic.201500524. Epub 2016 Mar 11.

Crystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound Form.

Author information

1
Department of Biochemistry, Saarland University, Campus B2.2, 66123, Saarbrücken, Germany.
2
Department of Structural Biology, ZHMB, Saarland University, Building 60, 66421, Homburg, Germany.
3
Center for Bioinformatics, Saarland University, Campus E2.1, 66123, Saarbrücken, Germany.
4
Department of Biochemistry, Saarland University, Campus B2.2, 66123, Saarbrücken, Germany. ritabern@mx.uni-saarland.de.

Abstract

CYP106A2 from Bacillus megaterium ATCC 13368 is known as a bacterial steroid hydroxylase that is also capable of hydroxylating a variety of terpenoids. To analyze the substrate specificity of this enzyme further, different resin acids of the abietane and pimarane types were tested with regard to binding and conversion. Product formation could be shown for all tested substrates. Spectroscopic studies revealed type I binding spectra for isopimaric acid, but dehydroabietic acid did not induce a high-spin shift of the enzyme. Interestingly, binding of abietic acid resulted in a type II difference spectrum typical for nitrogenous inhibitors. Co-crystallization of CYP106A2 with abietic acid and structure determination revealed bending of the heme cofactor when abietic acid was bound in the active site. Quantum chemical calculations strongly suggest that this heme distortion is the cause of the unusual spectroscopic characteristics.

KEYWORDS:

CYP106A2; X-ray diffraction; abietic acid; heme distortion; oxidoreductases

PMID:
26864272
DOI:
10.1002/cbic.201500524
[Indexed for MEDLINE]

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