AI Article Synopsis
- Geranyl-CoA carboxylase (GCC) is crucial for the growth of Pseudomonas bacteria using geranic acid as their only carbon source.
- The crystal structure of GCC shows similarities to 3-methylcrotonyl-CoA carboxylase (MCC) but notable differences from propionyl-CoA carboxylase (PCC), supporting separate evolutionary paths for these enzymes.
- Specific structural differences, particularly a glycine-to-phenylalanine mutation in the active site, explain why GCC and MCC have different substrate preferences, suggesting that altering this residue can switch their substrate choices.
Article 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4673880 | PMC |
| http://dx.doi.org/10.1038/ncomms9986 | DOI Listing |
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