ArticleCommunications biology2026
Architecture of an asymmetric short chain/long chain hybrid acyl‑CoA carboxylase from Mycobacterium smegmatis.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
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4 authors.
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Abstract
Mycobacteria comprise an uneven number of genes coding for biotin carboxylase (BC) and acyl-CoA carboxyl transferase (CT) activities and an ε-subunit of unknown function. To unravel the composition of acyl-CoA carboxylase (ACCase) holoenzymes under native conditions, we pulled down endogenously expressed biotinylated proteins from Mycobacterium smegmatis. The extract included an unexpected 16-subunit ACCase holoenzyme, exhibiting distinct long-chain (LC) and short-chain (SC) CT activities. It consists of a central two-layered CT (AccD4)₂/(AccD5)₄ assembly that interacts with a C-terminal AccE5 dimer within its central hole. On each CT hexamer face, an asymmetric BC AccA3 tetramer is connected through a flexible AccE5 segment. This is preceded by a folded AccE5 segment that contributes to an asymmetric nine-stranded β-barrel with contributions from all four AccA3 subunits. This barrel allows the BC assembly to rotate ~90
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