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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-65DF-5 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-DB73-8
Genre: Journal Article

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 Creators:
Kühnel, Karin1, Author           
Ke, Na, Author
Cryle, Max1, Author           
Sligar, Stephen G., Author
Schuler, Mary A., Author
Schlichting, Ilme1, Author           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 2008-04-222008-02-262008-05-312008-05-312008-06-24
 Publication Status: Issued
 Pages: 8
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi800328s
URI: http://www.ncbi.nlm.nih.gov/pubmed/18512957
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 47 (25) Sequence Number: - Start / End Page: 6552 - 6559 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103