Reexamination of the Three-Dimensional Structure of the Small Subunit of RuBisCo from Higher Plants

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Science  12 May 1989:
Vol. 244, Issue 4905, pp. 702-705
DOI: 10.1126/science.244.4905.702


The structure of L8S8 RuBisCo (where L is the large subunit and S is the small subunit) from spinach has been determined to a resolution of 2.8 ångstrom by using fourfold averaging of an isomorphous electron density map based on three heavy-atom derivatives. The structure of the S subunit is different from that previously reported for the tobacco S subunit in spite of 75 percent sequence identity. The elements of secondary structure, four antiparallel β strands and two α helices, are the same, but the topology and direction of the polypeptide chain through these elements differ completely. One of these models is clearly wrong. The spinach model has hydrophobic residues in the core between the α helices and β sheet as well as conserved residues in the subunit interactions. The deletion of residues 49 to 62 that is present in the Anabaena sequence removes a loop region in the spinach model. The positions of three mercury atoms in the heavy-atom derivatives agree with the assignment of side chains in the spinach structure.

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