9CD3

Cryo-EM structure of Candidatus Saccharibacterium phosphoketolase complexed with thiamine diphosphate

Summary for 9CD3

• Entry DOI: 10.2210/pdb9cd3/pdb
• EMDB information: 45461
• Descriptor: Phosphoketolase family protein, THIAMINE DIPHOSPHATE (2 entities in total)
• Functional Keywords: acetyl-phosphate synthase, glycolaldehyde dehydration, carbohydrate metabolic process, aldehyde-lyase activity, lyase
• Biological source: Candidatus Saccharibacteria bacterium
• Total number of polymer chains: 2
• Total formula weight: 181464.96

Authors

Singal, B.,Landwehr, G.,Jewett, M.C. (deposition date: 2024-06-24, release date: 2025-08-06, Last modification date: 2025-11-26)

Primary citation

Landwehr, G.M.,Vogeli, B.,Tian, C.,Singal, B.,Gupta, A.,Lion, R.,Sargent, E.H.,Karim, A.S.,Jewett, M.C.
A synthetic cell-free pathway for biocatalytic upgrading of one-carbon substrates.
Biorxiv, 2024

PubMed Abstract: Biotechnological processes hold tremendous potential for the efficient and sustainable conversion of one-carbon (C1) substrates into complex multi-carbon products. However, the development of robust and versatile biocatalytic systems for this purpose remains a significant challenge. In this study, we report a hybrid electrochemical-biochemical cell-free system for the conversion of C1 substrates into the universal biological building block acetyl-CoA. The synthetic reductive formate pathway (ReForm) consists of five core enzymes catalyzing non-natural reactions that were established through a cell-free enzyme engineering platform. We demonstrate that ReForm works in a plug-and-play manner to accept diverse C1 substrates including CO equivalents. We anticipate that ReForm will facilitate efforts to build and improve synthetic C1 utilization pathways for a formate-based bioeconomy.

PubMed: 39149402
DOI: 10.1101/2024.08.08.607227

Experimental method

ELECTRON MICROSCOPY (2.18 Å)