Reexamination of the three-dimensional structure of the small subunit of RuBisCo from higher plants
1989
Knight, S. | Andersson, I. | Branden, C.I.
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 angstrom 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 beta strands and two alpha 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 alpha helices and beta 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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