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Crystal structures of substrate-free and retinoic acid-bound cyanobacterial cytochrome P450 CYP120A1

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Kühnel,  Karin
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Cryle,  Max
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Kühnel, K., Ke, N., Cryle, M., Sligar, S. G., Schuler, M. A., & Schlichting, I. (2008). Crystal structures of substrate-free and retinoic acid-bound cyanobacterial cytochrome P450 CYP120A1. Biochemistry, 47(25), 6552-6559. doi:10.1021/bi800328s.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-65DF-5
Abstract
The crystal structures of substrate-free and all-trans-retinoic acid-bound CYP120A1 from Synechocystis sp. PCC 6803 were determined at 2.4 and 2.1 A resolution, respectively, representing the first structural characterization of a cyanobacterial P450. Features of CYP120A1 not observed in other P450 structures include an aromatic ladder flanking the channel leading to the active site and a triple-glycine motif within SRS5. Using spectroscopic methods, CYP120A1 is shown to bind 13-cis-retinoic acid, 9-cis-retinoic acid, and retinal with high affinity and dissociation constants of less than 1 microM. Metabolism of retinoic acid by CYP120A1 suggests that CYP120A1 hydroxylates a variety of retinoid derivatives in vivo. On the basis of the retinoic acid-bound CYP120A1 crystal structure, we propose that either carbon 2 or the methyl groups (C16 or C17) of the beta-ionone ring are modified by CYP120A1.