Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex

Schneidewind, Judith; Bocola, Marco; Davari, Mehdi D.; Krause, Frank; Krauss, Ulrich; Jaeger, Karl-Erich; Stadler, Andreas Maximilian; Schwaneberg, Ulrich

doi:10.1038/s42003-019-0590-4

Journal Article

FZJ-2019-04514

Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex

Schneidewind, J.FZJ* ; Krause, F. ; Bocola, M. ; Stadler, A. M.FZJ* ; Davari, M. D. ; Schwaneberg, U. ; Jaeger, K.-E.FZJ* ; Krauss, U. (Corresponding author)FZJ*

2019
Springer Nature London

Communications biology 2(1), 351 (2019) [10.1038/s42003-019-0590-4]

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Please use a persistent id in citations: http://hdl.handle.net/2128/23451 doi:10.1038/s42003-019-0590-4

Abstract: 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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