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000864911 1001_ $$0P:(DE-Juel1)161384$$aSchneidewind, Judith$$b0$$ufzj
000864911 245__ $$aConsensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
000864911 260__ $$aLondon$$bSpringer Nature$$c2019
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000864911 520__ $$aPhotosynthetic organisms employ two different enzymes for the reduction of the C17 = C18 double bond of protochlorophyllide (Pchlide), yielding the chlorophyll precursor chlorophyllide. First, a nitrogenase-like, light-independent (dark-operative) Pchlide oxidoreductase and secondly, a light-dependent Pchlide oxidoreductase (LPOR). For the latter enzyme, despite decades of research, no structural information is available. Here, we use protein structure modelling, molecular dynamics (MD) simulations combined with multi-wavelength analytical ultracentrifugation (MWA-AUC) and small angle X-ray scattering (SAXS) experiments to derive a consensus model of the LPOR apoprotein and the substrate/cofactor/LPOR ternary complex. MWA-AUC and SAXS experiments independently demonstrate that the apoprotein is monomeric, while ternary complex formation induces dimerization. SAXS-guided modelling studies provide a full-length model of the apoprotein and suggest a tentative mode of dimerization for the LPOR ternary complex, supported by published cross-link constraints. Our study provides a first impression of the LPOR structural organization.
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000864911 7001_ $$0P:(DE-HGF)0$$aKrause, Frank$$b1
000864911 7001_ $$0P:(DE-HGF)0$$aBocola, Marco$$b2
000864911 7001_ $$0P:(DE-Juel1)140278$$aStadler, Andreas Maximilian$$b3
000864911 7001_ $$0P:(DE-HGF)0$$aDavari, Mehdi D.$$b4
000864911 7001_ $$0P:(DE-HGF)0$$aSchwaneberg, Ulrich$$b5
000864911 7001_ $$0P:(DE-Juel1)131457$$aJaeger, Karl-Erich$$b6
000864911 7001_ $$0P:(DE-Juel1)131482$$aKrauss, Ulrich$$b7$$eCorresponding author
000864911 773__ $$0PERI:(DE-600)2919698-X$$a10.1038/s42003-019-0590-4$$gVol. 2, no. 1, p. 351$$n1$$p351$$tCommunications biology$$v2$$x2399-3642$$y2019
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