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Structure of a hyperthermostable dimeric archaeal Rubisco from Hyperthermus butylicus
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Bundela, Rudranuj, Keown, Jeremy R., Watkin, Serena and Pearce, Frederick Grant (2019) Structure of a hyperthermostable dimeric archaeal Rubisco from Hyperthermus butylicus. Acta Crystallographica Section D Structural Biology, 75 (6). pp. 536-544. doi:10.1107/S2059798319006466 ISSN 2059-7983.
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Official URL: http://doi.org/10.1107/S2059798319006466
Abstract
The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from the hyperthermophilic archaeon Hyperthermus butylicus 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, H. butylicus 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, H. butylicus Rubisco presents a well characterized system in which to investigate the role of assembly and thermal stability in enzyme function.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Acta Crystallographica Section D Structural Biology | ||||
Publisher: | International Union of Crystallography | ||||
ISSN: | 2059-7983 | ||||
Official Date: | 1 June 2019 | ||||
Dates: |
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Volume: | 75 | ||||
Number: | 6 | ||||
Page Range: | pp. 536-544 | ||||
DOI: | 10.1107/S2059798319006466 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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