Journal
STRUCTURE
Volume 18, Issue 10, Pages 1300-1310Publisher
CELL PRESS
DOI: 10.1016/j.str.2010.07.008
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Funding
- Department of Industry, Tourism and Trade of the Government of the Autonomous Community of the Basque Country
- Innovation Technology Department of the Bizkaia County
- National Institutes of Health [DK067238]
- Caja Navarra [16507]
- NIH [GM008798]
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Pyruvate carboxylase (PC) is a conserved multifunctional enzyme linked to important metabolic diseases. PC homotetramer is arranged in two layers with two opposing monomers per layer. Cryo-EM explores the conformational variability of PC in the presence of different substrates. The results demonstrate that the biotin-carboxyl carrier protein (BCCP) domain localizes near the biotin carboxylase (BC) domain of its own monomer and travels to the carboxyltransferase (CT) domain of the opposite monomer. All density maps show noticeable conformational differences between layers, mainly for the BCCP and BC domains. This asymmetry may be indicative of a coordination mechanism where monomers from different layers catalyze the BC and CT reactions consecutively. A conformational change of the PC tetramerization (PT) domain suggests a new functional role in communication. A long-range communication pathway between subunits in different layers, via interacting PT-PT and BC-BC domains, may be responsible for the cooperativity of PC from Staphylococcus aureus.
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