6sgw | pdb_00006sgw

Structure of the ESX-3 core complex

Loading... Status: waiting for Mol* initialization Structural highlights 6sgw is a 10 chain structure with sequence from Mycs2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: eccB3, MSMEG_0616, MSMEI_0600 (MYCS2), eccD3, snm, MSMEG_0623, MSMEI_0607 (MYCS2), eccC3, MSMEG_0617, MSMEI_0601 (MYCS2), eccE3, MSMEG_0626, MSMEI_0609 (MYCS2) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ECCE3_MYCS2] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG. [ECCB3_MYCS2] An ATPase (By similarity). Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.[UniProtKB:P9WNR7] [ECCC3_MYCS2] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG. [ECCD3_MYCS2] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG. Publication Abstract from PubMed Host infection by pathogenic mycobacteria such as Mycobacterium tuberculosis is facilitated by virulence factors secreted by type VII secretion systems(1). Here we report the cryo-electron microscopy structure of a membrane-embedded core complex of the ESX-3/type VII secretion system from Mycobacterium smegmatis at 3.7 A resolution. The core of the ESX-3 secretion machine consists of four protein components, EccB3:EccC3:EccD3:EccE3 in a 1:1:2:1 stoichiometry, building two identical protomers. The EccC3 coupling protein comprises a flexible array of four ATPase domains, which are linked to the membrane through a stalk domain. The 'domain of unknown function' (DUF) adjacent to the stalk is identified as an ATPase domain essential for secretion. EccB3 is predominantly periplasmatic but a small segment crosses the membrane and contacts the stalk domain, suggesting that conformational changes in the stalk domain triggered by substrate binding at the distal end of EccC3 and subsequent ATP hydrolysis in the DUF could be coupled to substrate secretion to the periplasm. Our results reveal that the architecture of type VII secretion systems differs markedly from other known secretion machines(2). Architecture of the mycobacterial type VII secretion system.,Famelis N, Rivera-Calzada A, Degliesposti G, Wingender M, Mietrach N, Skehel JM, Fernandez-Leiro R, Bottcher B, Schlosser A, Llorca O, Geibel S Nature. 2019 Oct 9. pii: 10.1038/s41586-019-1633-1. doi:, 10.1038/s41586-019-1633-1. PMID:31597161 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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