6hr8 | pdb_00006hr8

HMG-CoA reductase from Methanothermococcus thermolithotrophicus in complex with NADPH at 2.9 A resolution

spinqualitylabelsall models 6hr8, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hr8 is a 6 chain structure with sequence from Methanothermococcus thermolithotrophicus atcc 35097. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA, NAP, PEG, SO4 NonStd Res: CSO Gene: HMGR (Methanothermococcus thermolithotrophicus ATCC 35097) Activity: Hydroxymethylglutaryl-CoA reductase (NADPH), with EC number 1.1.1.34 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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