This title appears in the Scientific Report :
2019
Please use the identifier:
http://hdl.handle.net/2128/23451 in citations.
Please use the identifier: http://dx.doi.org/10.1038/s42003-019-0590-4 in citations.
Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
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-depende...
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Personal Name(s): | Schneidewind, Judith |
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Krause, Frank / Bocola, Marco / Stadler, Andreas Maximilian / Davari, Mehdi D. / Schwaneberg, Ulrich / Jaeger, Karl-Erich / Krauss, Ulrich (Corresponding author) | |
Contributing Institute: |
Neutronenstreuung; ICS-1 Neutronenstreuung; JCNS-1 Institut für Molekulare Enzymtechnologie (HHUD); IMET Biotechnologie; IBG-1 |
Published in: | Communications biology, 2 (2019) 1, S. 351 |
Imprint: |
London
Springer Nature
2019
|
DOI: |
10.1038/s42003-019-0590-4 |
PubMed ID: |
31583285 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology |
Link: |
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Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1038/s42003-019-0590-4 in citations.
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. |