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-Structure paper
タイトル | Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 7999, Year 2023 |
掲載日 | 2023年12月4日 |
著者 | Jianwei Li / Xin Xu / Jian Shi / Juan A Hermoso / Lok-To Sham / Min Luo / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:38044344 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.9 - 5.7 Å |
構造データ | EMDB-35362, PDB-8idb: EMDB-35363, PDB-8idc: EMDB-35364, PDB-8idd: EMDB-35437, PDB-8igq: EMDB-36304, PDB-8jia: |
化合物 | ChemComp-ATP: ChemComp-ADP: |
由来 |
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キーワード | TRANSPORT PROTEIN / complex |