5IKL

Crystal structure of P. aeruginosa geranyl-CoA carboxylase (GCC), beta subunit

Summary for 5IKL

• Entry DOI: 10.2210/pdb5ikl/pdb
• Descriptor: Geranyl-CoA carboxylase, beta-subunit (2 entities in total)
• Functional Keywords: carboxylase, organic acid metabolism, ligase
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
• Total number of polymer chains: 3
• Total formula weight: 171789.42

Authors

Huang, C.S.,Jurado, A.R.,Tong, L. (deposition date: 2016-03-03, release date: 2016-04-13, Last modification date: 2024-03-06)

Primary citation

Jurado, A.R.,Huang, C.S.,Zhang, X.,Zhou, Z.H.,Tong, L.
Structure and substrate selectivity of the 750-kDa alpha6beta6 holoenzyme of geranyl-CoA carboxylase
Nat Commun, 6:1-8, 2015

PubMed 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.

PubMed: 26593090
DOI: 10.1038/ncomms9986

Experimental method

X-RAY DIFFRACTION (2.4 Å)