8CIW
Methylsuccinyl-CoA dehydrogenase from Pseudomonas migulae with bound FAD and (2S)-methylsuccinyl-CoA
Summary for 8CIW
| Entry DOI | 10.2210/pdb8ciw/pdb |
| Descriptor | (2S)-methylsuccinyl-CoA dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, (2S)-Methylsuccinyl-CoA, ... (7 entities in total) |
| Functional Keywords | fad, dehydrogenase, methylsuccinyl-coa, oxidoreductase |
| Biological source | Pseudomonas migulae |
| Total number of polymer chains | 2 |
| Total formula weight | 124256.19 |
| Authors | Zarzycki, J.,McLean, R.,Erb, T.J. (deposition date: 2023-02-10, release date: 2023-07-12, Last modification date: 2024-06-19) |
| Primary citation | McLean, R.,Schwander, T.,Diehl, C.,Cortina, N.S.,Paczia, N.,Zarzycki, J.,Erb, T.J. Exploring alternative pathways for the in vitro establishment of the HOPAC cycle for synthetic CO 2 fixation. Sci Adv, 9:eadh4299-eadh4299, 2023 Cited by PubMed Abstract: Nature has evolved eight different pathways for the capture and conversion of CO, including the Calvin-Benson-Bassham cycle of photosynthesis. Yet, these pathways underlie constrains and only represent a fraction of the thousands of theoretically possible solutions. To overcome the limitations of natural evolution, we introduce the HydrOxyPropionyl-CoA/Acrylyl-CoA (HOPAC) cycle, a new-to-nature CO-fixation pathway that was designed through metabolic retrosynthesis around the reductive carboxylation of acrylyl-CoA, a highly efficient principle of CO fixation. We realized the HOPAC cycle in a step-wise fashion and used rational engineering approaches and machine learning-guided workflows to further optimize its output by more than one order of magnitude. Version 4.0 of the HOPAC cycle encompasses 11 enzymes from six different organisms, converting ~3.0 mM CO into glycolate within 2 hours. Our work moves the hypothetical HOPAC cycle from a theoretical design into an established in vitro system that forms the basis for different potential applications. PubMed: 37315145DOI: 10.1126/sciadv.adh4299 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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