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Science 1 July 1988:
Vol. 241. no. 4861, pp. 71 - 74
DOI: 10.1126/science.3133767
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Articles

Science, Vol 241, Issue 4861, 71-74
Copyright © 1988 by American Association for the Advancement of Science

articles

Tertiary structure of plant RuBisCO: domains and their contacts

MS Chapman, SW Suh, PM Curmi, D Cascio, WW Smith, and DS Eisenberg

Molecular Biology Institute, University of California, Los Angeles 90024.

The three-dimensional structure of ribulose-1,5-biphosphate carboxylase-oxygenase (RuBisCO), has been determined at 2.6 A resolution. This enzyme initiates photosynthesis by combining carbon dioxide with ribulose bisphosphate to form two molecules of 3-phosphoglycerate. In plants, RuBisCO is built from eight large (L) and eight small (S) polypeptide chains, or subunits. Both S chains and the NH2-terminal domain (N) of L are antiparallel beta, "open-face-sandwich" domains with four-stranded beta sheets and flanking alpha helices. The main domain (B) of L is an alpha/beta barrel containing most of the catalytic residues. The active site is in a pocket at the opening of the barrel that is partly covered by the N domain of a neighboring L chain. The domain contacts of the molecule and its conserved residues are discussed in terms of this structure.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Science. ISSN 0036-8075 (print), 1095-9203 (online)