Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1
| العنوان: | Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1 |
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| المؤلفون: | Hao-Ping Chen, Aye Aye Khine, Kai-Fa Huang, Tzu Ping Ko |
| المصدر: | Acta Crystallographica. Section F, Structural Biology Communications |
| بيانات النشر: | International Union of Crystallography (IUCr), 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | Protein Conformation, alpha-Helical, Rossmann fold, Stereochemistry, Monoterpene, Biophysics, Reductase, medicine.disease_cause, Biochemistry, Research Communications, Substrate Specificity, Borneol, 03 medical and health sciences, chemistry.chemical_compound, X-Ray Diffraction, Tetramer, camphor, Structural Biology, Pseudomonas, Lysogeny broth, Escherichia coli, Genetics, medicine, plant terpenoids, Amino Acid Sequence, 030304 developmental biology, 0303 health sciences, Camphanes, biology, 030306 microbiology, protein solubility, NAD, Condensed Matter Physics, biology.organism_classification, Recombinant Proteins, oxidoreductases, expression medium, Alcohol Oxidoreductases, chemistry, Protein Conformation, beta-Strand, Protein Multimerization, Protein Binding |
| الوصف: | The structure of a Pseudomonas borneol dehydrogenase was determined at 1.84 Å resolution. Major differences from its homologues in the C-terminal helices and the associated loops may suggest determinants for substrate recognition. During the microbial degradation of borneol, a bicyclic plant monoterpene, it is first converted into camphor by borneol dehydrogenase (BDH) and then enters a known camphor-degradation pathway. Previously, a recombinant Pseudomonas BDH was found in inclusion bodies when expressed in Escherichia coli. After refolding, it was still unstable and was difficult to concentrate. Here, the protein-expression conditions were improved by changing the medium from lysogeny broth to Terrific Broth, yielding a soluble form of the enzyme with higher activity. The protein was crystallized and its 3D structure was determined by X-ray diffraction. Like other known homologues such as quinuclidinone reductase, the protein forms a tetramer with subunits containing Rossmann folds. Structural comparison revealed major differences in the C-terminal helices and the associated loops. It is likely that these regions contain the determinants for substrate recognition. |
| تدمد: | 2053-230X |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::765b3f12f1b483a3f615bd12e5d1e37d https://doi.org/10.1107/s2053230x20008584 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....765b3f12f1b483a3f615bd12e5d1e37d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 2053230X |
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