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<jats:p>The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from the hyperthermophilic archaeon <jats:italic>Hyperthermus butylicus</jats:italic> is presented at 1.8 Å resolution. Previous structures of archaeal Rubisco have been found to assemble into decamers, and this oligomerization was thought to be required for a highly thermally stable enzyme. In the current study, <jats:italic>H. butylicus</jats:italic> Rubisco is shown to exist as a dimer in solution, yet has a thermal denaturation midpoint of 114°C, suggesting that high thermal stability can be achieved without an increased oligomeric state. This increased thermal stability appears to be due to an increased number of electrostatic interactions within the monomeric subunit. As such, <jats:italic>H. butylicus</jats:italic> Rubisco presents a well characterized system in which to investigate the role of assembly and thermal stability in enzyme function.</jats:p>

Original publication

DOI

10.1107/s2059798319006466

Type

Journal article

Journal

Acta Crystallographica Section D Structural Biology

Publisher

International Union of Crystallography (IUCr)

Publication Date

01/06/2019

Volume

75

Pages

536 - 544