6HR7

HMG-CoA reductase from Methanothermococcus thermolithotrophicus apo form at 2.4 A resolution

6HR7 の概要

• エントリーDOI: 10.2210/pdb6hr7/pdb
• 分子名称: HMG-CoA reductase, SULFATE ION, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (8 entities in total)
• 機能のキーワード: hmg-coa, mevalonate biosynthesis, statins, cholesterol biosynthesis, isoprenoids, structural rearrangement., oxidoreductase
• 由来する生物種: Methanothermococcus thermolithotrophicus DSM 2095
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94677.49

構造登録者

Wagner, T.,Voegeli, B.,Erb, T.J.,Shima, S. (登録日: 2018-09-26, 公開日: 2019-02-13, 最終更新日: 2024-01-24)

主引用文献

Vogeli, B.,Shima, S.,Erb, T.J.,Wagner, T.
Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme.
Febs Lett., 593:543-553, 2019

PubMed Abstract: 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyses the last step in mevalonate biosynthesis. HMGR is the target of statin inhibitors that regulate cholesterol concentration in human blood. Here, we report the properties and structures of HMGR from an archaeon Methanothermococcus thermolithotrophicus (mHMGR). The structures of the apoenzyme and the NADPH complex are highly similar to those of human HMGR. A notable exception is C-terminal helix (Lα10-11) that is straight in both mHMGR structures. This helix is kinked and closes the active site in the human enzyme ternary complex, pointing to a substrate-induced structural rearrangement of C-terminal in class-I HMGRs during the catalytic cycle.

PubMed: 30702149
DOI: 10.1002/1873-3468.13331

実験手法

X-RAY DIFFRACTION (2.4 Å)