8TEB
Structure of MKbur
8TEB の概要
| エントリーDOI | 10.2210/pdb8teb/pdb |
| 分子名称 | Mevalonate kinase, 1,2-ETHANEDIOL, CHLORIDE ION, ... (5 entities in total) |
| 機能のキーワード | extremo-tolerant, psychrophilic, transferase |
| 由来する生物種 | Methanococcoides burtonii |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 66294.25 |
| 構造登録者 | Peat, T.S.,Newman, J.,Esquirol, L.,Nebl, T.,Scott, C.,Vickers, C.,Sainsbury, F. (登録日: 2023-07-06, 公開日: 2024-03-13) |
| 主引用文献 | 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 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: 38411551DOI: 10.1107/S2059798324001360 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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