Download MendeleyCharacterization of novel mevalonate kinases from the tardigrade Ramazzottius varieornatus and the psychrophilic archaeon Methanococcoides burtonii.
Esquirol, L., Newman, J., Nebl, T., Scott, C., Vickers, C., Sainsbury, F., Peat, T.S.(2024) Acta Crystallogr D Struct Biol 80: 203-215
- PubMed: 38411551
- DOI: https://doi.org/10.1107/S2059798324001360
- Primary Citation of Related Structures:
8TEB, 8TFO - PubMed Abstract:
Mevalonate kinase is central to the isoprenoid biosynthesis pathway. Here, high-resolution X-ray crystal structures of two mevalonate kinases are presented: a eukaryotic protein from Ramazzottius varieornatus and an archaeal protein from Methanococcoides burtonii. Both enzymes possess the highly conserved motifs of the GHMP enzyme superfamily, with notable differences between the two enzymes in the N-terminal part of the structures. Biochemical characterization of the two enzymes revealed major differences in their sensitivity to geranyl pyrophosphate and farnesyl pyrophosphate, and in their thermal stabilities. This work adds to the understanding of the structural basis of enzyme inhibition and thermostability in mevalonate kinases.
Organizational Affiliation:
Environment, Commonwealth Scientific and Industrial Research Organisation, GPO Box 1700, Canberra, ACT 2601, Australia.
