1gvn

Crystal Structure of the Plasmid Maintenance System epsilon/zeta: Meachnism of toxin inactivation and toxin function

spinqualitylabelsall models 1gvn, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gvn is a 4 chain structure with sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EATX_STRPY Antitoxin component of a toxin-antitoxin (TA) module. Neutralizes the toxic effect of cognate zeta toxin. Part of a postsegregational killing (PSK) system involved in the killing of plasmid-free cells. Continuous synthesis of the epsilon antitoxin is required to counteract the zeta toxin.[REFERENCE:7] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Programmed cell death in prokaryotes is frequently found as postsegregational killing. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid. The broad-host-range, low-copy-number plasmid pSM19035 from Streptococcus pyogenes carries the genes encoding the antitoxin/toxin system epsilon/zeta and antibiotic resistance proteins, among others. The crystal structure of the biologically nontoxic epsilon(2)zeta(2) protein complex at a 1.95-A resolution and site-directed mutagenesis showed that free zeta acts as phosphotransferase by using ATPGTP. In epsilon(2)zeta(2), the toxin zeta is inactivated because the N-terminal helix of the antitoxin epsilon blocks the ATPGTP-binding site. To our knowledge, this is the first prokaryotic postsegregational killing system that has been entirely structurally characterized. Crystal structure of the plasmid maintenance system epsilon/zeta: functional mechanism of toxin zeta and inactivation by epsilon 2 zeta 2 complex formation.,Meinhart A, Alonso JC, Strater N, Saenger W Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1661-6. Epub 2003 Feb 5. PMID:12571357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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