8dsx | pdb_00008dsx

NMR STRUCTURE OF THE BACTERIOPHAGE LAMBDA EA22 C-TERMINAL DOMAIN

spinqualitylabelsall models 8dsx Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8dsx is a 2 chain structure with sequence from Escherichia virus Lambda. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EA22_LAMBD Publication Abstract from PubMed Enterohemorrhagic Escherichia coli (EHEC) outbreaks are commonly associated with contaminated food sources. Unlike normal intestinal bacteria, EHEC are lysogens of lambdoid bacteriophages that also carry a gene for Shiga toxin. Oxidative attack by the immune system or other stressors on the bacterial host can activate the lytic pathway of the latent phage genome to produce phage progeny and the release of Shiga toxin into the surrounding tissues. Within the genomes of bacteriophage lambda and Shiga toxin-expressing (Stx(+)) phages such as phi24(B) and phiP27, there is a conserved set of open reading frames that is located between the exo and xis genes that influences the lysogenic-lytic decision. In this report, we have focused on the largest exo-xis region open reading frame termed ea22 that has been shown previously to have prolysogenic properties. Using a variety of biophysical and bioinformatic methods, we demonstrate that lambda and phiP27 Ea22 proteins are tetrameric in solution and can be considered in terms of an amino-terminal region, a central coiled-coil region, and a carboxy-terminal region. The carboxy-terminal regions of lambda and phi24(B) Ea22, expressed on their own, form dimers with exceptional thermostability. Limited proteolysis of phiP27 Ea22 also identified a C-terminal region along the predicted boundaries. While the three Ea22 proteins all appear to have the hallmarks of a domain in their respective C-terminal regions, each sequence is remarkably dissimilar. To reconcile this difference among Ea22 proteins from lambda and Stx(+) phages alike, we speculate that each Ea22 may achieve the same function by targeting different components of the same regulatory process in the host. Ea22 Proteins from Lambda and Shiga Toxin-Producing Bacteriophages Balance Structural Diversity with Functional Similarity.,Tong J, Nejman-Falenczyk B, Bloch S, Wegrzyn A, Wegrzyn G, Donaldson LW ACS Omega. 2020 May 19;5(21):12236-12244. doi: 10.1021/acsomega.0c00894. , eCollection 2020 Jun 2. PMID:32548406 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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