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8TEB

Structure of MKbur

Summary for 8TEB
Entry DOI10.2210/pdb8teb/pdb
DescriptorMevalonate kinase, 1,2-ETHANEDIOL, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsextremo-tolerant, psychrophilic, transferase
Biological sourceMethanococcoides burtonii
Total number of polymer chains2
Total formula weight66294.25
Authors
Peat, T.S.,Newman, J.,Esquirol, L.,Nebl, T.,Scott, C.,Vickers, C.,Sainsbury, F. (deposition date: 2023-07-06, release date: 2024-03-13)
Primary citationEsquirol, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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