title: Subunit interface dynamics in hexadecameric rubisco.
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.
authors: Department of Molecular Biology, Swedish University of Agricultural Sciences, Box 590, S-75124 Uppsala, Sweden.
authors: Michiel
authors: M
authors: van Lun
authors: David
authors: D
authors: van der Spoel
authors: Inger
authors: I
authors: Andersson
mesh_terms: D002384:Catalysis; D016825:Chlamydomonas reinhardtii / Q000201:enzymology* / Q000235:genetics; D018360:Crystallography, X-Ray; D056004:Molecular Dynamics Simulation; D016297:Mutagenesis, Site-Directed; D009154:Mutation / Q000235:genetics; D011487:Protein Conformation; D055503:Protein Multimerization; D021122:Protein Subunits; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012274:Ribulosephosphates / Q000378:metabolism
chemical_list: D021122:Protein Subunits; D012274:Ribulosephosphates; C001933:ribulose-1,5 diphosphate; D012273:Ribulose-Bisphosphate Carboxylase