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

Author

Listed:
  • Christine S. Huang

    (Columbia University)

  • Kianoush Sadre-Bazzaz

    (Columbia University)

  • Yang Shen

    (Columbia University
    Present address: Department of Antibody Technology, ImClone Systems, 180 Varick Street, 6th Floor, New York, New York 10014, USA.)

  • Binbin Deng

    (University of Texas Medical School at Houston)

  • Z. Hong Zhou

    (University of Texas Medical School at Houston
    Immunology and Molecular Genetics, University of California, Los Angeles)

  • Liang Tong

    (Columbia University)

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.

Suggested Citation

  • Christine S. Huang & Kianoush Sadre-Bazzaz & Yang Shen & Binbin Deng & Z. Hong Zhou & Liang Tong, 2010. "Crystal structure of the α6β6 holoenzyme of propionyl-coenzyme A carboxylase," Nature, Nature, vol. 466(7309), pages 1001-1005, August.
    • Handle: RePEc:nat:nature:v:466:y:2010:i:7309:d:10.1038_nature09302
    DOI: 10.1038/nature09302
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    Cited by:

    1. Jorge Pedro López-Alonso & Melisa Lázaro & David Gil-Cartón & Philip H. Choi & Alexandra Dodu & Liang Tong & Mikel Valle, 2022. "CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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