Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex
dc.bibliographicCitation.firstPage | 351 | eng |
dc.bibliographicCitation.journalTitle | Communications biology | eng |
dc.bibliographicCitation.volume | 2 | eng |
dc.contributor.author | Schneidewind, Judith | |
dc.contributor.author | Krause, Frank | |
dc.contributor.author | Bocola, Marco | |
dc.contributor.author | Stadler, Andreas Maximilian | |
dc.contributor.author | Davari, Mehdi D. | |
dc.contributor.author | Schwaneberg, Ulrich | |
dc.contributor.author | Jaeger, Karl-Erich | |
dc.contributor.author | Krauss, Ulrich | |
dc.date.accessioned | 2022-01-17T09:08:34Z | |
dc.date.available | 2022-01-17T09:08:34Z | |
dc.date.issued | 2019 | |
dc.description.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. | eng |
dc.description.version | publishedVersion | eng |
dc.identifier.uri | https://oa.tib.eu/renate/handle/123456789/7824 | |
dc.identifier.uri | https://doi.org/10.34657/6865 | |
dc.language.iso | eng | eng |
dc.publisher | London : Springer Nature | eng |
dc.relation.doi | https://doi.org/10.1038/s42003-019-0590-4 | |
dc.relation.essn | 2399-3642 | |
dc.rights.license | CC BY 4.0 Unported | eng |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | eng |
dc.subject.ddc | 570 | eng |
dc.subject.other | apoprotein | eng |
dc.subject.other | oxidoreductase | eng |
dc.subject.other | pigment | eng |
dc.subject.other | protochlorophyllide reductase | eng |
dc.subject.other | chemical structure | eng |
dc.subject.other | chemistry | eng |
dc.subject.other | cyanobacterium | eng |
dc.subject.other | metabolism | eng |
dc.subject.other | molecular model | eng |
dc.subject.other | photosynthesis | eng |
dc.subject.other | physiology | eng |
dc.subject.other | protein multimerization | eng |
dc.subject.other | structure activity relation | eng |
dc.subject.other | Apoproteins | eng |
dc.subject.other | Cyanobacteria | eng |
dc.subject.other | Models, Molecular | eng |
dc.subject.other | Molecular Structure | eng |
dc.subject.other | Oxidoreductases Acting on CH-CH Group Donors | eng |
dc.subject.other | Photosynthesis | eng |
dc.subject.other | Pigments, Biological | eng |
dc.subject.other | Protein Multimerization | eng |
dc.subject.other | Structure-Activity Relationship | eng |
dc.title | Consensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complex | eng |
dc.type | Article | eng |
dc.type | Text | eng |
tib.accessRights | openAccess | eng |
wgl.contributor | DWI | eng |
wgl.subject | Biowissensschaften/Biologie | eng |
wgl.type | Zeitschriftenartikel | eng |
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