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Research article2011Peer reviewed

Subunit Interface Dynamics in Hexadecameric Rubisco

Van Lun, Michiel; van der Spoel, David; Andersson, Inger

Abstract

Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) plays an important role in the global carbon cycle as a hub for biomass. Rubisco catalyzes not only the carboxylation of RuBP with carbon dioxide but also a competing oxygenation reaction of RuBP with a negative impact on photosynthetic yield. The functional active site is built from two large (L) subunits that form a dimer. The octameric core of four L(2) dimers is held at each end by a cluster of four small (S) subunits, forming a hexadecamer. Each large subunit contacts more than one S subunit. These interactions exploit the dynamic flexibility of Rubisco, which we address in this study. Here, we describe seven different types of interfaces of hexadecameric Rubisco. We have analyzed these interfaces with respect to the size of the interface area and the number of polar interactions, including salt bridges and hydrogen bonds in a variety of Rubisco enzymes from different organisms and different kingdoms of life, including the Rubisco-like proteins. We have also performed molecular dynamics simulations of Rubisco from Chlamydomonas reinhardtii and mutants thereof. From our computational analyses, we propose structural checkpoints of the S subunit to ensure the functionality and/or assembly of the Rubisco holoenzyme. These checkpoints appear to fine-tune the dynamics of the enzyme in a way that could influence enzyme performance. (C) 2011 Elsevier Ltd. All rights reserved.

Keywords

ribulose-1,5-bisphosphate carboxylase/oxygenase; Rubisco; subunit interface; inter-subunit contacts; molecular dynamics simulations

Published in

Journal of Molecular Biology
2011, Volume: 411, number: 5, pages: 1083-1098
Publisher: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD

      SLU Authors

    • Van Lun, Michiel

      • Department of Molecular Biology, Swedish University of Agricultural Sciences
      • Andersson, Inger

        • Department of Molecular Biology, Swedish University of Agricultural Sciences

      UKÄ Subject classification

      Environmental Sciences related to Agriculture and Land-use
      Forest Science
      Agricultural Science

      Publication identifier

      DOI: https://doi.org/10.1016/j.jmb.2011.06.052

      Permanent link to this page (URI)

      https://res.slu.se/id/publ/57704