Active E. coli heteromeric acetyl-CoA carboxylase forms polymorphic helical tubular filaments.

Autor:	Xu X; Department of Biological Sciences, Purdue University; West Lafayette, IN 47907 USA., de Sousa AS; Department of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824 USA.; Department of Biochemistry, Purdue University; West Lafayette, IN 47907 USA., Boram TJ; Department of Biochemistry, Purdue University; West Lafayette, IN 47907 USA., Jiang W; Department of Biological Sciences, Purdue University; West Lafayette, IN 47907 USA., Lohman JR; Department of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824 USA.; Department of Biochemistry, Purdue University; West Lafayette, IN 47907 USA.
Jazyk:	angličtina
Zdroj:	BioRxiv : the preprint server for biology [bioRxiv] 2024 May 28. Date of Electronic Publication: 2024 May 28.
DOI:	10.1101/2024.05.28.596234
Abstrakt:	The Escherichia coli heteromeric acetyl-CoA carboxylase (ACC) has four subunits assumed to form an elusive catalytic complex and are involved in allosteric and transcriptional regulation. The E. coli ACC represents almost all ACCs from pathogenic bacteria making it a key antibiotic development target to fight growing antibiotic resistance. Furthermore, it is a model for cyanobacterial and plant plastid ACCs as biofuel engineering targets. Here we report the catalytic E. coli ACC complex surprisingly forms tubes rather than dispersed particles. The cryo-EM structure reveals key protein-protein interactions underpinning efficient catalysis and how transcriptional regulatory roles are masked during catalysis. Discovering the protein-protein interaction interfaces that facilitate catalysis, allosteric and transcriptional regulation provides new routes to engineering catalytic activity and new targets for drug discovery. Competing Interests: Competing interests: Authors declare that they have no competing interests.
Databáze:	MEDLINE
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