دورية أكاديمية
أعرض في EDS

Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.

التفاصيل البيبلوغرافية
العنوان: Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
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
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-023-43770-6