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  A structural model of PpoA derived from SAXS-analysis-Implications for substrate conversion.

Koch, C., Tria, G., Fielding, A., Brodhun, F., Valerius, O., Feussner, K., et al. (2013). A structural model of PpoA derived from SAXS-analysis-Implications for substrate conversion. Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 1831(9), 1449-1457. doi:10.1016/j.bbalip.2013.06.003.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-4DEB-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1D5F-6
Genre: Journal Article

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 Creators:
Koch, C., Author
Tria, G., Author
Fielding, A.1, Author              
Brodhun, F., Author
Valerius, O., Author
Feussner, K., Author
Braus, G. H., Author
Svergun, D. I., Author
Bennati, M.1, Author              
Feussner, I., Author
Affiliations:
1Research Group of Electron Paramagnetic Resonance, MPI for biophysical chemistry, Max Planck Society, ou_578606              

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Free keywords: Cytochrome P450; Dioxygenase; Double electron-electron resonance; Oxylipin; Psi-factor producing oxygenase; Small-angle X-ray scattering
 Abstract: In plants and mammals, oxylipins may be synthesized via multi step processes that consist of dioxygenation and isomerization of the intermediately formed hydroperoxy fatty acid. These processes are typically catalyzed by two distinct enzyme classes: dioxygenases and cytochrome P450 enzymes. In ascomycetes biosynthesis of oxylipins may proceed by a similar two-step pathway. An important difference, however, is that both enzymatic activities may be combined in a single bifunctional enzyme. These types of enzymes are named Psi-factor producing oxygenases (Ppo). Here, the spatial organization of the two domains of PpoA from Aspergillus nidulans was analyzed by small-angle X-ray scattering and the obtained data show that the enzyme exhibits a relatively flat trimeric shape. Atomic structures of the single domains were obtained by template-based structure prediction and docked into the enzyme envelope of the low resolution structure obtained by SAXS. EPR-based distance measurements between the tyrosyl radicals formed in the activated dioxygenase domain of the enzyme supported the trimeric structure obtained from SAXS and the previous assignment of Tyr374 as radical-site in PpoA. Furthermore, two phenylalanine residues in the cytochrome P450 domain were shown to modulate the specificity of hydroperoxy fatty acid rearrangement.

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Language(s): eng - English
 Dates: 2013-06-212013-09
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bbalip.2013.06.003
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Title: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Source Genre: Journal
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Pages: - Volume / Issue: 1831 (9) Sequence Number: - Start / End Page: 1449 - 1457 Identifier: -