Nature 337, 229 - 234 (19 January 1989); doi:10.1038/337229a0

Crystal structure of the active site of ribulose-bisphosphate carboxylase

Inger Andersson^*, Stefan Knight^*, Gunter Schneider^*, Ylva Lindqvist^*, Tomas Lundqvist^*, Carl-Ivar Brändén^* & George H. Lorimer^†

^* Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, PO Box 590, S-75124 Uppsala, Sweden
^† Central Research and Development Department, E. I. du Pont de Nemours and Co., Wilmington, Delaware 19898, USA

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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