ArticleChembiochem : a European journal of chemical biology2013
Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus.
Article in Chembiochem : a European journal of chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- LipoproteinmBio · 2025Article
- The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.Extremophiles : life under extreme conditions · 2022Review
- Hexamerization and thermostability emerged very early during geranylgeranylglyceryl phosphate synthase evolution.Protein science : a publication of the Protein Society · 2021Article
- Structural studies of geranylgeranylglyceryl phosphate synthase, a prenyltransferase found in thermophilic Euryarchaeota.Acta crystallographica. Section D, Structural biology · 2020Article
- Construction of an artificial biosynthetic pathway for hyperextended archaeal membrane lipids in the bacteriumSynthetic biology (Oxford, England) · 2020Article
- Identification and Characterization of Heptaprenylglyceryl Phosphate Processing Enzymes in Bacillus subtilis.The Journal of biological chemistry · 2016Article
- Constitutive Activation of the Nlrc4 Inflammasome Prevents Hepatic Fibrosis and Promotes Hepatic Regeneration after Partial Hepatectomy.Mediators of inflammation · 2015Article
- A re-evaluation of the archaeal membrane lipid biosynthetic pathway.Nature reviews. Microbiology · 2014Review
- Biosynthesis of archaeal membrane ether lipids.Frontiers in microbiology · 2014Review
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Authors and funding
14 authors.
Funding
Abstract
Well structured: As a new triose phosphate isomerase (TIM) barrel-fold prenyl transferase, PcrB catalyzes the production of heptaprenylglyceryl phosphate from heptaprenyl diphosphate and glycerol-1-phosphate. Crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus in complex with ligands were solved, and together with site-directed mutagenesis and bioinformatics analyses, clearly reveal the catalytic mechanism of the enzyme.
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