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TitleA structural model of PpoA derived from SAXS-analysis-implications for substrate conversion.
Journal, issue, pagesBiochim Biophys Acta, Vol. 1831, Issue 9, Page 1449-1457, Year 2013
Publish dateJun 21, 2013
AuthorsChristian Koch / Giancarlo Tria / Alistair J Fielding / Florian Brodhun / Oliver Valerius / Kirstin Feussner / Gerhard H Braus / Dmitri I Svergun / Marina Bennati / Ivo Feussner /
PubMed AbstractIn 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 ...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.
External linksBiochim Biophys Acta / PubMed:23797010
MethodsSAS (X-ray synchrotron)
Structure data

SASDA45:
PpoA wild type enzyme (Psi-producing oxygenase A, PpoA)
Method: SAXS/SANS

Source
  • Aspergillus nidulans (mold)

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