A distinct holoenzyme organization for two-subunit pyruvate carboxylase.

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 α₄β₄ stoichiometry. We report here the crystal structures of a two-subunit PC from Methylobacillus flagellatus. Surprisingly, our structures reveal an α₂β₄ stoichiometry, and the overall architecture of the holoe

SUBMITTER: Choi PH 

PROVIDER: S-EPMC5059739 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature