ArticleBiochemistry2018
Structural Features and Domain Movements Controlling Substrate Binding and Cofactor Specificity in Class II HMG-CoA Reductase.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- A cofactor-promiscuous HMGR from the Lyme disease pathogen illuminates diversity in bacterial isoprenoid biosynthesis.Protein science : a publication of the Protein Society · 2026Article
- A cofactor-promiscuous HMGR from the Lyme disease pathogen illuminates diversity in bacterial isoprenoid biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Emerging roles of the metabolic regulator 3-hydroxy-3-methylglutaryl coenzyme-CoA reductase in human cancers: From biology to therapeutics.Genes & diseases · 2026Review
- Unique kinetic behavior of a secondary alcohol dehydrogenase: from a reaction engineering point of view.Bioprocess and biosystems engineering · 2026Article
- Harnessing evolution: leveraging bacterial isoprenoid pathway diversity toward improved bioengineering strategies.Journal of bacteriology · 2026Review
- Integrated Multi-Omics Investigation of Gypenosides' Mechanisms in Lowering Hepatic Cholesterol.Biomolecules · 2025Article
- Improving Cofactor Promiscuity of HMG-CoA Reductase fromBiomolecules · 2025Article
- Identifying Opportunity Targets in Gram-Negative Pathogens for Infectious Disease Mitigation.ACS central science · 2025Review
- pH-dependent reaction triggering in PmHMGR crystals for time-resolved crystallography.Biophysical journal · 2024Article
- Targeting Enterococcus faecalis HMG-CoA reductase with a non-statin inhibitor.Communications biology · 2023Article
- A fungal tolerance trait and selective inhibitors proffer HMG-CoA reductase as a herbicide mode-of-action.Nature communications · 2022Article
- Antibacterial Effect of Some Eukaryotic Sterol Biosynthesis Inhibitors.Advanced biomedical research · 2022Article
- An Atomic-Level Perspective of HMG-CoA-Reductase: The Target Enzyme to Treat Hypercholesterolemia.Molecules (Basel, Switzerland) · 2020Review
- [Blood lipid metabolic profile of overweight/obese boys aged 9-12 years].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2020Article
- Debottlenecking mevalonate pathway for antimalarial drug precursor amorphadiene biosynthesis inMetabolic engineering communications · 2020Article
- New Crystallographic Snapshots of Large Domain Movements in Bacterial 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase.Biochemistry · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The key mevalonate pathway enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (HMGR) uses the cofactor NAD(P)H to reduce HMG-CoA to mevalonate in the production of countless metabolites and natural products. Although inhibition of HMGR by statin drugs is well-understood, several mechanistic details of HMGR catalysis remain unresolved, and the structural basis for the wide range of cofactor specificity for either NADH or NADPH among HMGRs from different organisms is also unknown. Here, we present crystal structures of HMGR from Streptococcus pneumoniae (SpHMGR) alongside kinetic data of the enzyme's cofactor preferences. Our structure of SpHMGR bound with its kinetically preferred NADPH cofactor suggests how NADPH-specific binding and recognition are achieved. In addition, our structure of HMG-CoA-bound SpHMGR reveals large, previously unknown conformational domain movements that may control HMGR substrate binding and enable cofactor exchange without intermediate release during the catalytic cycle. Taken together, this work provides critical new insights into both the HMGR reaction mechanism and the structural basis of cofactor specificity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.