4n8n

Crystal structure of Mycobacterial FtsX extracellular domain

spinqualitylabelsall models 4n8n, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n8n is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: K Related: 4n8o Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FTSX_MYCTU] Part of the ABC transporter FtsEX involved in cellular division (By similarity). Publication Abstract from PubMed Bacterial growth and cell division are coordinated with hydrolysis of the peptidoglycan (PG) layer of the cell wall, but the mechanisms of regulation of extracellular PG hydrolases are not well understood. Here we report the biochemical, structural, and genetic analysis of the Mycobacterium tuberculosis homolog of the transmembrane PG-hydrolase regulator, FtsX. The purified FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme. Deletion of ftsEX and ripC caused similar phenotypes in Mycobacterium smegmatis, as expected for genes in a single pathway. The crystal structure of the FtsX extracellular domain reveals an unprecedented fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes reduce RipC binding in vitro and inhibit FtsX function in M. smegmatis. These studies suggest how FtsX recognizes RipC and support a model in which a conformational change in FtsX links the cell division apparatus with PG hydrolysis. Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC.,Mavrici D, Marakalala MJ, Holton JM, Prigozhin DM, Gee CL, Zhang YJ, Rubin EJ, Alber T Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8037-42. doi:, 10.1073/pnas.1321812111. Epub 2014 May 19. PMID:24843173 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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