6hun
Dimeric Archeal Rubisco from Hyperthermus butylicusDimeric Archeal Rubisco from Hyperthermus butylicus
Structural highlights
FunctionA2BK54_HYPBU Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.[HAMAP-Rule:MF_01133] Publication Abstract from PubMedThe crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from the hyperthermophilic archaeon Hyperthermus butylicus is presented at 1.8 A 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 degrees 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. Structure of a hyperthermostable dimeric archaeal Rubisco from Hyperthermus butylicus.,Bundela R, Keown J, Watkin S, Pearce FG Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):536-544. doi:, 10.1107/S2059798319006466. Epub 2019 May 28. PMID:31205016[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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