دورية أكاديمية
A morpheein equilibrium regulates catalysis in phosphoserine phosphatase SerB2 from Mycobacterium tuberculosis.
| العنوان: | A morpheein equilibrium regulates catalysis in phosphoserine phosphatase SerB2 from Mycobacterium tuberculosis. |
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| المؤلفون: | Pierson, Elise, De Pol, Florian, Fillet, Marianne, Wouters, Johan |
| المساهمون: | CIRM - Centre Interdisciplinaire de Recherche sur le Médicament - ULiège, BE |
| المصدر: | Communications Biology, 6 (1), 1024 (2023-10-10) |
| بيانات النشر: | Nature Research, 2023. |
| سنة النشر: | 2023 |
| مصطلحات موضوعية: | phosphoserine phosphatase, Phosphoric Monoester Hydrolases, Phosphoric Monoester Hydrolases/metabolism, Catalysis, Mycobacterium tuberculosis/genetics, Mycobacterium tuberculosis/metabolism, Mycobacterium tuberculosis, Medicine (miscellaneous), Biochemistry, Genetics and Molecular Biology (all), Agricultural and Biological Sciences (all), General Agricultural and Biological Sciences, General Biochemistry, Genetics and Molecular Biology, Human health sciences, Pharmacy, pharmacology & toxicology, Sciences de la santé humaine, Pharmacie, pharmacologie & toxicologie |
| الوصف: | Mycobacterium tuberculosis phosphoserine phosphatase MtSerB2 is of interest as a new antituberculosis target due to its essential metabolic role in L-serine biosynthesis and effector functions in infected cells. Previous works indicated that MtSerB2 is regulated through an oligomeric transition induced by L-Ser that could serve as a basis for the design of selective allosteric inhibitors. However, the mechanism underlying this transition remains highly elusive due to the lack of experimental structural data. Here we describe a structural, biophysical, and enzymological characterisation of MtSerB2 oligomerisation in the presence and absence of L-Ser. We show that MtSerB2 coexists in dimeric, trimeric, and tetrameric forms of different activity levels interconverting through a conformationally flexible monomeric state, which is not observed in two near-identical mycobacterial orthologs. This morpheein behaviour exhibited by MtSerB2 lays the foundation for future allosteric drug discovery and provides a starting point to the understanding of its peculiar multifunctional moonlighting properties. |
| نوع الوثيقة: | journal article http://purl.org/coar/resource_type/c_6501Test article peer reviewed |
| اللغة: | English |
| العلاقة: | https://www.nature.com/articles/s42003-023-05402-z.pdfTest; urn:issn:2399-3642 |
| DOI: | 10.1038/s42003-023-05402-z |
| الوصول الحر: | https://orbi.uliege.be/handle/2268/315493Test |
| حقوق: | open access http://purl.org/coar/access_right/c_abf2Test info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsorb.315493 |
| قاعدة البيانات: | ORBi |
| DOI: | 10.1038/s42003-023-05402-z |
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