ArticleThe Journal of biological chemistry2015
Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ·LysW complex from Thermus thermophilus.
Article in The Journal of biological chemistry, 2015. 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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9 citing papers in PubMed, 17 citations in OpenAlex.
- Evolution of lysine and arginine biosynthesis revealed by substrate specificity of lysine biosynthetic enzymes in Thermus thermophilus.The FEBS journal · 2026Article
- Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.FEBS letters · 2025Article
- Dissecting the Arginine and Lysine Biosynthetic Pathways and Their Relationship in Haloarchaeon Natrinema gari J7-2 via Endogenous CRISPR-Cas System-Based Genome Editing.Microbiology spectrum · 2023Article
- Biosynthesis of 3-thia-α-amino acids on a carrier peptide.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Heterologous gene expression and characterization of two serine hydroxymethyltransferases from Thermoplasma acidophilum.Extremophiles : life under extreme conditions · 2021Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Amino-group carrier-protein-mediated secondary metabolite biosynthesis in Streptomyces.Nature chemical biology · 2016Article
- Lysine Biosynthesis of Thermococcus kodakarensis with the Capacity to Function as an Ornithine Biosynthetic System.The Journal of biological chemistry · 2016Article
- Crystal Structure of the LysY·LysW Complex from Thermus thermophilus.The Journal of biological chemistry · 2016Article
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6 authors at 2 institutions in 1 country.
Funding
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Abstract
In the biosynthesis of lysine by Thermus thermophilus, the metabolite α-ketoglutarate is converted to the intermediate α-aminoadipate (AAA), which is protected by the 54-amino acid acidic protein LysW. In this study, we determined the crystal structure of LysZ from T. thermophilus (TtLysZ), an amino acid kinase that catalyzes the second step in the AAA to lysine conversion, which was in a complex with LysW at a resolution of 1.85 Å. A crystal analysis coupled with isothermal titration calorimetry of the TtLysZ mutants for TtLysW revealed tight interactions between LysZ and the globular and C-terminal extension domains of the LysW protein, which were mainly attributed to electrostatic forces. These results provided structural evidence for LysW acting as a protecting molecule for the α-amino group of AAA and also as a carrier protein to guarantee better recognition by biosynthetic enzymes for the efficient biosynthesis of lysine.
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