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| 100 | 1 | _ | |a Schneidewind, Judith |0 P:(DE-Juel1)161384 |b 0 |u fzj |
| 245 | _ | _ | |a Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex |
| 260 | _ | _ | |a London |c 2019 |b Springer Nature |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1578400760_25426 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 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. |
| 536 | _ | _ | |a 581 - Biotechnology (POF3-581) |0 G:(DE-HGF)POF3-581 |c POF3-581 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef |
| 700 | 1 | _ | |a Krause, Frank |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Bocola, Marco |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Stadler, Andreas Maximilian |0 P:(DE-Juel1)140278 |b 3 |
| 700 | 1 | _ | |a Davari, Mehdi D. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Schwaneberg, Ulrich |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Jaeger, Karl-Erich |0 P:(DE-Juel1)131457 |b 6 |
| 700 | 1 | _ | |a Krauss, Ulrich |0 P:(DE-Juel1)131482 |b 7 |e Corresponding author |
| 773 | _ | _ | |a 10.1038/s42003-019-0590-4 |g Vol. 2, no. 1, p. 351 |0 PERI:(DE-600)2919698-X |n 1 |p 351 |t Communications biology |v 2 |y 2019 |x 2399-3642 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/864911/files/Invoice%202676157050.pdf |
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| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/864911/files/s42003-019-0590-4.pdf |y OpenAccess |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/864911/files/s42003-019-0590-4.pdf?subformat=pdfa |x pdfa |y OpenAccess |
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