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The unique allosteric property of crocodilian haemoglobin elucidated by cryo-EM

Author

Listed:
  • Katsuya Takahashi

    (Yokohama City University)

  • Yongchan Lee

    (Yokohama City University)

  • Angela Fago

    (Aarhus University)

  • Naim M. Bautista

    (University of Nebraska)

  • Jay F. Storz

    (University of Nebraska)

  • Akihiro Kawamoto

    (Osaka University)

  • Genji Kurisu

    (Osaka University)

  • Tomohiro Nishizawa

    (Yokohama City University)

  • Jeremy R. H. Tame

    (Yokohama City University)

Abstract

The principal effect controlling the oxygen affinity of vertebrate haemoglobins (Hbs) is the allosteric switch between R and T forms with relatively high and low oxygen affinity respectively. Uniquely among jawed vertebrates, crocodilians possess Hb that shows a profound drop in oxygen affinity in the presence of bicarbonate ions. This allows them to stay underwater for extended periods by consuming almost all the oxygen present in the blood-stream, as metabolism releases carbon dioxide, whose conversion to bicarbonate and hydrogen ions is catalysed by carbonic anhydrase. Despite the apparent universal utility of bicarbonate as an allosteric regulator of Hb, this property evolved only in crocodilians. We report here the molecular structures of both human and a crocodilian Hb in the deoxy and liganded states, solved by cryo-electron microscopy. We reveal the precise interactions between two bicarbonate ions and the crocodilian protein at symmetry-related sites found only in the T state. No other known effector of vertebrate Hbs binds anywhere near these sites.

Suggested Citation

  • Katsuya Takahashi & Yongchan Lee & Angela Fago & Naim M. Bautista & Jay F. Storz & Akihiro Kawamoto & Genji Kurisu & Tomohiro Nishizawa & Jeremy R. H. Tame, 2024. "The unique allosteric property of crocodilian haemoglobin elucidated by cryo-EM," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49947-x
    DOI: 10.1038/s41467-024-49947-x
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    References listed on IDEAS

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    1. Mark A. Herzik & Mengyu Wu & Gabriel C. Lander, 2019. "High-resolution structure determination of sub-100 kDa complexes using conventional cryo-EM," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
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