5n8n | pdb_00005n8n

Contracted sheath of a Pseudomonas aeruginosa type six secretion system consisting of TssB1 and TssC1

spinqualitylabelsall models 5n8n, resolution 3.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n8n is a 30 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: AO964_32215, PAERUG_E15_London_28_01_14_04448, PAERUG_P32_London_17_VIM_2_10_11_02574, PAMH19_0082 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885), U769_00445 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Pseudomonas aeruginosa has three type VI secretion systems (T6SSs), H1-, H2-, and H3-T6SS, each belonging to a distinct group. The two T6SS components, TssB/VipA and TssC/VipB, assemble to form tubules that conserve structural/functional homology with tail sheaths of contractile bacteriophages and pyocins. Here, we used cryoelectron microscopy to solve the structure of the H1-T6SS P. aeruginosa TssB1C1 sheath at 3.3 A resolution. Our structure allowed us to resolve some features of the T6SS sheath that were not resolved in the Vibrio cholerae VipAB and Francisella tularensis IglAB structures. Comparison with sheath structures from other contractile machines, including T4 phage and R-type pyocins, provides a better understanding of how these systems have conserved similar functions/mechanisms despite evolution. We used the P. aeruginosa R2 pyocin as a structural template to build an atomic model of the TssB1C1 sheath in its extended conformation, allowing us to propose a coiled-spring-like mechanism for T6SS sheath contraction. Atomic Structure of Type VI Contractile Sheath from Pseudomonas aeruginosa.,Salih O, He S, Planamente S, Stach L, MacDonald JT, Manoli E, Scheres SHW, Filloux A, Freemont PS Structure. 2017 Dec 21. pii: S0969-2126(17)30404-5. doi:, 10.1016/j.str.2017.12.005. PMID:29307484 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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