دورية أكاديمية
Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
العنوان: | Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis. |
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المؤلفون: | Li J; Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore., Xu X; Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore., Shi J; Center for Bioimaging Sciences, Department of Biological Sciences, National University of Singapore, Singapore, Singapore., Hermoso JA; Department of Crystallography and Structural Biology, Instituto de Química-Física 'Blas Cabrera', Consejo Superior de Investigaciones Científicas, Madrid, Spain. xjuan@iqfr.csic.es., Sham LT; Infectious Diseases Translational Research Programme and Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore. lsham@nus.edu.sg., Luo M; Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore. dbslmin@nus.edu.sg.; Center for Bioimaging Sciences, Department of Biological Sciences, National University of Singapore, Singapore, Singapore. dbslmin@nus.edu.sg. |
المصدر: | Nature communications [Nat Commun] 2023 Dec 04; Vol. 14 (1), pp. 7999. Date of Electronic Publication: 2023 Dec 04. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: [London] : Nature Pub. Group |
مواضيع طبية MeSH: | Cell Cycle Proteins*/metabolism , Mycobacterium tuberculosis*/genetics , Mycobacterium tuberculosis*/metabolism, Humans ; Hydrolases ; Bacterial Proteins/metabolism ; Peptidoglycan/metabolism ; Cell Division |
مستخلص: | The FtsEX complex regulates, directly or via a protein mediator depending on bacterial genera, peptidoglycan degradation for cell division. In mycobacteria and Gram-positive bacteria, the FtsEX system directly activates peptidoglycan-hydrolases by a mechanism that remains unclear. Here we report our investigation of Mycobacterium tuberculosis FtsEX as a non-canonical regulator with high basal ATPase activity. The cryo-EM structures of the FtsEX system alone and in complex with RipC, as well as the ATP-activated state, unveil detailed information on the signal transduction mechanism, leading to the activation of RipC. Our findings indicate that RipC is recognized through a "Match and Fit" mechanism, resulting in an asymmetric rearrangement of the extracellular domains of FtsX and a unique inclined binding mode of RipC. This study provides insights into the molecular mechanisms of FtsEX and RipC regulation in the context of a critical human pathogen, guiding the design of drugs targeting peptidoglycan remodeling. (© 2023. The Author(s).) |
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معلومات مُعتمدة: | 22-3449-A0001 Ministry of Education - Singapore (MOE); 22-3448-A0001 Ministry of Education - Singapore (MOE); MOE-T2EP30222-0015 Ministry of Education - Singapore (MOE) |
المشرفين على المادة: | 0 (Cell Cycle Proteins) EC 3.- (Hydrolases) 0 (Bacterial Proteins) 0 (Peptidoglycan) |
تواريخ الأحداث: | Date Created: 20231203 Date Completed: 20231205 Latest Revision: 20231206 |
رمز التحديث: | 20240628 |
مُعرف محوري في PubMed: | PMC10694151 |
DOI: | 10.1038/s41467-023-43770-6 |
PMID: | 38044344 |
قاعدة البيانات: | MEDLINE |
تدمد: | 2041-1723 |
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DOI: | 10.1038/s41467-023-43770-6 |