4fxi | pdb_00004fxi

Crystal structure of the isolated E. coli RelE toxin, P21 form

spinqualitylabelsall models 4fxi, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fxi is a 3 chain structure with sequence from Escherichia coli k-12. This structure supersedes the now removed PDB entry 3kha. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: CME Related: 3kha, 2kc8, 2kc9 Gene: b1563, JW1555, relE (Escherichia coli K-12) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The bacterial relBE locus encodes a toxin-antitoxin complex in which the toxin, RelE, is capable of cleaving mRNA in the ribosomal A site cotranslationally. The antitoxin, RelB, both binds and inhibits RelE, and regulates transcription through operator binding and conditional cooperativity controlled by RelE. Here, we present the crystal structure of the intact Escherichia coli RelB2E2 complex at 2.8 A resolution, comprising both the RelB-inhibited RelE and the RelB dimerization domain that binds DNA. RelE and RelB associate into a V-shaped heterotetrameric complex with the ribbon-helix-helix (RHH) dimerization domain at the apex. Our structure supports a model in which relO is optimally bound by two adjacent RelB2E heterotrimeric units, and is not compatible with concomitant binding of two RelB2E2 heterotetramers. The results thus provide a firm basis for understanding the model of conditional cooperativity at the molecular level. The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity.,Boggild A, Sofos N, Andersen KR, Feddersen A, Easter AD, Passmore LA, Brodersen DE Structure. 2012 Oct 10;20(10):1641-8. doi: 10.1016/j.str.2012.08.017. Epub 2012, Sep 13. PMID:22981948 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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