8jia | pdb_00008jia

Cryo-EM structure of Mycobacterium tuberculosis ATP bound FtsE(E165Q)X/RipC complex in peptidisc

spinqualitylabelsall models 8jia, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8jia is a 5 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.9Å Ligands: ATP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTSE_MYCTU Part of the ABC transporter FtsEX involved in cellular division. Has ATPase activity.[UniProtKB:A5U7B7][UniProtKB:P0A9R7] Publication Abstract from PubMed 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. Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.,Li J, Xu X, Shi J, Hermoso JA, Sham LT, Luo M Nat Commun. 2023 Dec 4;14(1):7999. doi: 10.1038/s41467-023-43770-6. PMID:38044344 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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