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  Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme

Voegeli, B., Shima, S., Erb, T. J., & Wagner, T. (2019). Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme. FEBS LETTERS, 593(5), 543-553. doi:10.1002/1873-3468.13331.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0008-D638-8 Version Permalink: https://hdl.handle.net/21.11116/0000-0008-E20E-A
Genre: Journal Article

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 Creators:
Voegeli, Bastian1, Author           
Shima, Seigo2, Author           
Erb, Tobias J.1, Author           
Wagner, Tristan2, Author           
Affiliations:
1Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, Karl-von-Frisch-Strasse 10, D-35043 Marburg, DE, ou_3266303              
2Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, Karl-von-Frisch-Strasse 10, D-35043 Marburg, DE, ou_3266277              

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 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 (L alpha 10-11) 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.

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 Dates: 2019
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: ISI: 000461017900009
DOI: 10.1002/1873-3468.13331
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Title: FEBS LETTERS
Source Genre: Journal
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Pages: - Volume / Issue: 593 (5) Sequence Number: - Start / End Page: 543 - 553 Identifier: ISSN: 0014-5793