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A distinct holoenzyme organization for two-subunit pyruvate carboxylase

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  • Philip H. Choi

    (Columbia University)

  • Jeanyoung Jo

    (Columbia University)

  • Yu-Cheng Lin

    (Columbia University)

  • Min-Han Lin

    (National Yang-Ming University)

  • Chi-Yuan Chou

    (National Yang-Ming University)

  • Lars E. P. Dietrich

    (Columbia University)

  • Liang Tong

    (Columbia University)

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 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.

Suggested Citation

  • Philip H. Choi & Jeanyoung Jo & Yu-Cheng Lin & Min-Han Lin & Chi-Yuan Chou & Lars E. P. Dietrich & Liang Tong, 2016. "A distinct holoenzyme organization for two-subunit pyruvate carboxylase," Nature Communications, Nature, vol. 7(1), pages 1-13, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12713
    DOI: 10.1038/ncomms12713
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