2h28

Crystal structure of YeeU from E. coli. Northeast Structural Genomics target ER304

spinqualitylabelsall models 2h28, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h28 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, GOL, MG NonStd Res: MSE Gene: yeeU ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function [CBEA_ECOLI] Antitoxin component of a type IV toxin-antitoxin (TA) module. Labile antitoxin that counteracts the effect of its cognate toxin CbtA (YeeV). It does not bind to the toxin but instead binds to MreB and FtsZ (the toxin targets), enhancing their polymerization by forming higher-order bundles; it is probably retained in the MreB and FtsZ filament bundles. The mechanism has been proposed to require intergenic DNA, in cis, between the cbeA (yeeU) and cbta (yeeV) genes (PubMed:14594833). The intergenic region was not found to be necessary in another study (PubMed:22515815). Also counteracts the morphological defects caused by overexpression of SulA and DicB on cell shape. 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 Bacterial toxin-antitoxin (TA) systems serve a variety of physiological functions including regulation of cell growth and maintenance of foreign genetic elements. Sequence analyses suggest that TA families are linked by complex evolutionary relationships reflecting likely swapping of functional domains between different TA families. Our crystal structures of Phd-Doc from bacteriophage P1, the HigA antitoxin from Escherichia coli CFT073, and YeeU of the YeeUWV systems from E. coli K12 and Shigella flexneri confirm this inference and reveal additional, unanticipated structural relationships. The growth-regulating Doc toxin exhibits structural similarity to secreted virulence factors that are toxic for eukaryotic target cells. The Phd antitoxin possesses the same fold as both the YefM and NE2111 antitoxins that inhibit structurally unrelated toxins. YeeU, which has an antitoxin-like activity that represses toxin expression, is structurally similar to the ribosome-interacting toxins YoeB and RelE. These observations suggest extensive functional exchanges have occurred between TA systems during bacterial evolution. Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems.,Arbing MA, Handelman SK, Kuzin AP, Verdon G, Wang C, Su M, Rothenbacher FP, Abashidze M, Liu M, Hurley JM, Xiao R, Acton T, Inouye M, Montelione GT, Woychik NA, Hunt JF Structure. 2010 Aug 11;18(8):996-1010. PMID:20696400 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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