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8CIW

Methylsuccinyl-CoA dehydrogenase from Pseudomonas migulae with bound FAD and (2S)-methylsuccinyl-CoA

Summary for 8CIW
Entry DOI10.2210/pdb8ciw/pdb
Descriptor(2S)-methylsuccinyl-CoA dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, (2S)-Methylsuccinyl-CoA, ... (7 entities in total)
Functional Keywordsfad, dehydrogenase, methylsuccinyl-coa, oxidoreductase
Biological sourcePseudomonas migulae
Total number of polymer chains2
Total formula weight124256.19
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 citationMcLean, 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: 37315145
DOI: 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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