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024 7 _ |a 10.1038/s42003-019-0590-4
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100 1 _ |a Schneidewind, Judith
|0 P:(DE-Juel1)161384
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245 _ _ |a Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
260 _ _ |a London
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|b Springer Nature
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520 _ _ |a Photosynthetic 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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700 1 _ |a Krause, Frank
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700 1 _ |a Bocola, Marco
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700 1 _ |a Stadler, Andreas Maximilian
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700 1 _ |a Davari, Mehdi D.
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700 1 _ |a Schwaneberg, Ulrich
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700 1 _ |a Jaeger, Karl-Erich
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700 1 _ |a Krauss, Ulrich
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|e Corresponding author
773 _ _ |a 10.1038/s42003-019-0590-4
|g Vol. 2, no. 1, p. 351
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|p 351
|t Communications biology
|v 2
|y 2019
|x 2399-3642
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