6HR8
HMG-CoA reductase from Methanothermococcus thermolithotrophicus in complex with NADPH at 2.9 A resolution
Summary for 6HR8
| Entry DOI | 10.2210/pdb6hr8/pdb |
| Descriptor | HMG-CoA reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | hmg-coa, mevalonate biosynthesis, statins, cholesterol biosynthesis, isoprenoids, nadph, structural rearrangement., oxidoreductase |
| Biological source | Methanothermococcus thermolithotrophicus DSM 2095 More |
| Total number of polymer chains | 6 |
| Total formula weight | 285794.62 |
| Authors | Wagner, T.,Voegeli, B.,Erb, T.J.,Shima, S. (deposition date: 2018-09-26, release date: 2019-02-13, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 30702149DOI: 10.1002/1873-3468.13331 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
