5KS8

Crystal structure of two-subunit pyruvate carboxylase from Methylobacillus flagellatus

Summary for 5KS8

• Entry DOI: 10.2210/pdb5ks8/pdb
• Descriptor: Pyruvate carboxylase subunit alpha, Pyruvate carboxylase subunit beta, 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL, ... (5 entities in total)
• Functional Keywords: biotin, ligase, tim barrel, pyruvate
• Biological source: Methylobacillus flagellatus; More
• Total number of polymer chains: 6
• Total formula weight: 358940.13

Authors

Choi, P.H.,Tong, L. (deposition date: 2016-07-07, release date: 2016-10-19, Last modification date: 2024-04-03)

Primary citation

Choi, P.H.,Jo, J.,Lin, Y.C.,Lin, M.H.,Chou, C.Y.,Dietrich, L.E.,Tong, L.
A distinct holoenzyme organization for two-subunit pyruvate carboxylase.
Nat Commun, 7:12713-12713, 2016

PubMed Abstract: Pyruvate carboxylase (PC) has important roles in metabolism and is crucial for virulence for some pathogenic bacteria. PC contains biotin carboxylase (BC), carboxyltransferase (CT) and biotin carboxyl carrier protein (BCCP) components. It is a single-chain enzyme in eukaryotes and most bacteria, and functions as a 500 kD homo-tetramer. In contrast, PC is a two-subunit enzyme in a collection of Gram-negative bacteria, with the α subunit containing the BC and the β subunit the CT and BCCP domains, and it is believed that the holoenzyme has αβ stoichiometry. We report here the crystal structures of a two-subunit PC from Methylobacillus flagellatus. Surprisingly, our structures reveal an αβ stoichiometry, and the overall architecture of the holoenzyme is strikingly different from that of the homo-tetrameric PCs. Biochemical and mutagenesis studies confirm the stoichiometry and other structural observations. Our functional studies in Pseudomonas aeruginosa show that its two-subunit PC is important for colony morphogenesis.

PubMed: 27708276
DOI: 10.1038/ncomms12713

Experimental method

X-RAY DIFFRACTION (3.01 Å)