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Crystal structure of the active site of ribulose-bisphosphate carboxylase

Nature volume 337, pages 229–234 (1989)Cite this article

Abstract

Ribulose-bisphosphate carboxylase catalyses the key carboxylation reaction of photosynthetic carbon fixation, but also the competing oxygenase reaction of photorespiration. The structure of the active site of ribulose-bisphosphate carboxylase described here should provide a rational basis for attempts to improve the efficiency of the enzyme by genetic engineering.

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Authors and Affiliations

  1. Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, PO Box 590, Uppsala, S-75124, Sweden

    Inger Andersson, Stefan Knight, Gunter Schneider, Ylva Lindqvist, Tomas Lundqvist & Carl-Ivar Brändén

  2. Central Research and Development Department, E. I. du Pont de Nemours and Co., Wilmington, Delaware, 19898, USA

    George H. Lorimer

Authors
  1. Inger Andersson
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  2. Stefan Knight
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  3. Gunter Schneider
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  4. Ylva Lindqvist
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  5. Tomas Lundqvist
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  6. Carl-Ivar Brändén
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  7. George H. Lorimer
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Andersson, I., Knight, S., Schneider, G. et al. Crystal structure of the active site of ribulose-bisphosphate carboxylase. Nature 337, 229–234 (1989). https://doi.org/10.1038/337229a0

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