Structural highlights
Publication Abstract from PubMed
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 the 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 (Lalpha10-11) 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. This article is protected by copyright. All rights reserved.
Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme.,Vogeli B, Shima S, Erb T, Wagner T FEBS Lett. 2019 Jan 31. doi: 10.1002/1873-3468.13331. PMID:30702149[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vogeli B, Shima S, Erb T, 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. 2019 Jan 31. doi: 10.1002/1873-3468.13331. PMID:30702149 doi:http://dx.doi.org/10.1002/1873-3468.13331
