%0 Journal Article
%A Schneidewind, Judith
%A Krause, Frank
%A Bocola, Marco
%A Stadler, Andreas Maximilian
%A Davari, Mehdi D.
%A Schwaneberg, Ulrich
%A Jaeger, Karl-Erich
%A Krauss, Ulrich
%T Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
%J Communications biology
%V 2
%N 1
%@ 2399-3642
%C London
%I Springer Nature
%M FZJ-2019-04514
%P 351
%D 2019
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:31583285
%U <Go to ISI:>//WOS:000488309300001
%R 10.1038/s42003-019-0590-4
%U https://juser.fz-juelich.de/record/864911