The structure of propionyl-CoA carboxylase in the biotin carboxyl carrier protein UP state.

Abstract

Propionyl-CoA carboxylase (PCC) belongs to the biotin-dependent carboxylase family and plays a crucial role in mitochondria by catalyzing the conversion of propionyl-CoA to methylmalonyl-CoA. The product of PCC can enter the tricarboxylic acid (TCA) cycle, contributing to metabolic homeostasis. Impairment of PCC function can lead to several human metabolic diseases, but the mechanism and structure of PCC are not fully understood thus far. Here, we report the structure of human PCC at 3.64 Å, in which all biotin carboxyl carrier protein (BCCP) domains are swung up close to the biotin carboxylase (BC) domains. This structure provides insight into the catalytic mechanism of PCC.

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