TY  - JOUR
AU  - Schneidewind, Judith
AU  - Krause, Frank
AU  - Bocola, Marco
AU  - Stadler, Andreas Maximilian
AU  - Davari, Mehdi D.
AU  - Schwaneberg, Ulrich
AU  - Jaeger, Karl-Erich
AU  - Krauss, Ulrich
TI  - Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
JO  - Communications biology
VL  - 2
IS  - 1
SN  - 2399-3642
CY  - London
PB  - Springer Nature
M1  - FZJ-2019-04514
SP  - 351
PY  - 2019
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:31583285
UR  - <Go to ISI:>//WOS:000488309300001
DO  - DOI:10.1038/s42003-019-0590-4
UR  - https://juser.fz-juelich.de/record/864911
ER  -