ArticleThe Journal of biological chemistry2014
Crystal structure of the ectoine hydroxylase, a snapshot of the active site.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 38 citations in OpenAlex.
- Structural and mechanistic basis of sulfolytic C-S bond cleavage by an Fe(ii)/α-ketoglutarate-dependent sulfoquinovose dioxygenase.Chemical science · 2026Article
- Biosynthesis and import of the cytoprotective extremolytes ectoine and hydroxyectoine in the phylumFrontiers in microbiology · 2026Article
- Bioactivity profiling of the extremolyte ectoine as a promising protectant and its heterologous production.3 Biotech · 2022Review
- Genome analysis of the salt-resistant Paludifilum halophilum DSM 102817World journal of microbiology & biotechnology · 2021Article
- New insights into hydroxyectoine synthesis and its transcriptional regulation in the broad-salt growing halophilic bacterium Chromohalobacter salexigens.Microbial biotechnology · 2021Article
- Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase-deacetylase complex.The Journal of biological chemistry · 2020Article
- The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine.The Journal of biological chemistry · 2020Article
- Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis.Scientific reports · 2019Article
- Biosynthesis of the Stress-Protectant and Chemical Chaperon Ectoine: Biochemistry of the Transaminase EctB.Frontiers in microbiology · 2019Article
- Exploiting Substrate Promiscuity of Ectoine Hydroxylase for Regio- and Stereoselective Modification of Homoectoine.Frontiers in microbiology · 2019Article
- Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses.Natural product reports · 2018Review
- Review
- Tinkering with Osmotically Controlled Transcription Allows Enhanced Production and Excretion of Ectoine and Hydroxyectoine from a Microbial Cell Factory.Applied and environmental microbiology · 2018Article
- Compatible Solute Synthesis and Import by the Moderate HalophileFrontiers in microbiology · 2018Article
- Osmoadaptative Strategy and Its Molecular Signature in Obligately Halophilic Heterotrophic Protists.Genome biology and evolution · 2016Article
- EctD-mediated biotransformation of the chemical chaperone ectoine into hydroxyectoine and its mechanosensitive channel-independent excretion.Microbial cell factories · 2016Article
- Divergent non-heme iron enzymes in the nogalamycin biosynthetic pathway.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- Biochemistry and Crystal Structure of Ectoine Synthase: A Metal-Containing Member of the Cupin Superfamily.PloS one · 2016Article
- Overproduction, crystallization and X-ray diffraction data analysis of ectoine synthase from the cold-adapted marine bacterium Sphingopyxis alaskensis.Acta crystallographica. Section F, Structural biology communications · 2015Article
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5 authors at 3 institutions in 1 country.
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Abstract
Ectoine and its derivative 5-hydroxyectoine are compatible solutes that are widely synthesized by bacteria to cope physiologically with osmotic stress. They also serve as chemical chaperones and maintain the functionality of macromolecules. 5-Hydroxyectoine is produced from ectoine through a stereo-specific hydroxylation, an enzymatic reaction catalyzed by the ectoine hydroxylase (EctD). The EctD protein is a member of the non-heme-containing iron(II) and 2-oxoglutarate-dependent dioxygenase superfamily and is evolutionarily well conserved. We studied the ectoine hydroxylase from the cold-adapted marine ultra-microbacterium Sphingopyxis alaskensis (Sa) and found that the purified SaEctD protein is a homodimer in solution. We determined the SaEctD crystal structure in its apo-form, complexed with the iron catalyst, and in a form that contained iron, the co-substrate 2-oxoglutarate, and the reaction product of EctD, 5-hydroxyectoine. The iron and 2-oxoglutarate ligands are bound within the EctD active site in a fashion similar to that found in other members of the dioxygenase superfamily. 5-Hydroxyectoine, however, is coordinated by EctD in manner different from that found in high affinity solute receptor proteins operating in conjunction with microbial import systems for ectoines. Our crystallographic analysis provides a detailed view into the active site of the ectoine hydroxylase and exposes an intricate network of interactions between the enzyme and its ligands that collectively ensure the hydroxylation of the ectoine substrate in a position- and stereo-specific manner.
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