6suq

Crystal Structure of TcdB2-TccC3-TEV

spinqualitylabelsall models 6suq, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6suq is a 1 chain structure with sequence from Photorhabdus luminescens and Tobacco etch virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8GF97_PHOLU Q8GF99_PHOLU POLG_TEV Capsid protein: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication. Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication. Both 6K peptides are indispensable for virus replication (By similarity). Nuclear inclusion protein A: has RNA-binding and proteolytic activities. Publication Abstract from PubMed Tc toxins are bacterial protein complexes that inject cytotoxic enzymes into target cells using a syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxic enzyme. The toxic enzyme varies between Tc toxins from different species and is not conserved. Here, we investigate whether the toxic enzyme can be replaced by other small proteins of different origin and properties, namely Cdc42, herpes simplex virus ICP47, Arabidopsis thaliana iLOV, Escherichia coli DHFR, Ras-binding domain of CRAF kinase, and TEV protease. Using a combination of electron microscopy, X-ray crystallography and in vitro translocation assays, we demonstrate that it is possible to turn Tc toxins into customizable molecular syringes for delivering proteins of interest across membranes. We also infer the guidelines that protein cargos must obey in terms of size, charge, and fold in order to apply Tc toxins as a universal protein translocation system. Towards the application of Tc toxins as a universal protein translocation system.,Roderer D, Schubert E, Sitsel O, Raunser S Nat Commun. 2019 Nov 20;10(1):5263. doi: 10.1038/s41467-019-13253-8. PMID:31748551 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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