8TFO

Structure of MKvar

Summary for 8TFO

• Entry DOI: 10.2210/pdb8tfo/pdb
• Descriptor: Mevalonate kinase, (R)-MEVALONATE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: extremo-tolerant, psychrophilic, transferase
• Biological source: Ramazzottius varieornatus
• Total number of polymer chains: 2
• Total formula weight: 91226.30

Authors

Peat, T.S.,Newman, J.,Esquirol, L.,Nebl, T.,Scott, C.,Vickers, C.,Sainsbury, F. (deposition date: 2023-07-11, release date: 2024-03-13, Last modification date: 2024-10-16)

Primary citation

Esquirol, L.,Newman, J.,Nebl, T.,Scott, C.,Vickers, C.,Sainsbury, F.,Peat, T.S.
Characterization of novel mevalonate kinases from the tardigrade Ramazzottius varieornatus and the psychrophilic archaeon Methanococcoides burtonii.
Acta Crystallogr D Struct Biol, 80:203-215, 2024

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.

PubMed: 38411551
DOI: 10.1107/S2059798324001360

Experimental method

X-RAY DIFFRACTION (2 Å)