Crystal structure of the α6β6 holoenzyme of propionyl-coenzyme A carboxylase

Christine S. Huang, Kianoush Sadre-Bazzaz, Yang Shen, Binbin Deng, Z. Hong Zhou and Liang Tong ()
Additional contact information
Christine S. Huang: Columbia University
Kianoush Sadre-Bazzaz: Columbia University
Yang Shen: Columbia University
Binbin Deng: University of Texas Medical School at Houston
Z. Hong Zhou: University of Texas Medical School at Houston
Liang Tong: Columbia University

Nature, 2010, vol. 466, issue 7309, 1001-1005

Abstract: Propionyl-coenzyme A carboxylase structure The mitochondrial biotin-dependent enzyme propionyl-coenzyme A carboxylase (PCC) is essential for the catabolism of several amino acids, cholesterol and some fatty acids. The X-ray crystal and cryo-electron microscopy structures of the α6β6 dodecamer of PCC have now been determined. They reveal that the α-subunit contains the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains; the β-subunit is responsible for the carboxyltransferase activity. The BC domain and the carboxyltransferase domain are 55 ångströms apart, indicating that the BCCP domain must move a large distance during the catalytic cycle.

Date: 2010
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DOI: 10.1038/nature09302

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