ArticleNature communications2015
Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Biodegradation of poly(ester-urethane) coatings by Halopseudomonas formosensis.Microbial biotechnology · 2024Article
- Sample optimizations to enable the structure determination of biotin-dependent carboxylases.Methods in enzymology · 2024Article
- The opportunistic pathogen Pseudomonas aeruginosa exploits bacterial biotin synthesis pathway to benefit its infectivity.PLoS pathogens · 2023Article
- CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics.Journal of structural biology: X · 2023Article
- Article
- Crystal structure of the essential biotin-dependent carboxylase AccA3 fromFEBS open bio · 2017Article
- A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation.Cell discovery · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Geranyl-CoA carboxylase (GCC) is essential for the growth of Pseudomonas organisms with geranic acid as the sole carbon source. GCC has the same domain organization and shares strong sequence conservation with the related biotin-dependent carboxylases 3-methylcrotonyl-CoA carboxylase (MCC) and propionyl-CoA carboxylase (PCC). Here we report the crystal structure of the 750-kDa α6β6 holoenzyme of GCC, which is similar to MCC but strikingly different from PCC. The structures provide evidence in support of two distinct lineages of biotin-dependent acyl-CoA carboxylases, one carboxylating the α carbon of a saturated organic acid and the other carboxylating the γ carbon of an α-β unsaturated acid. Structural differences in the active site region of GCC and MCC explain their distinct substrate preferences. Especially, a glycine residue in GCC is replaced by phenylalanine in MCC, which blocks access by the larger geranyl-CoA substrate. Mutation of this residue in the two enzymes can change their substrate preferences.
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