3ez6 | pdb_00003ez6

Structure of parA-ADP complex:tetragonal form

spinqualitylabelsall models 3ez6, resolution 2.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ez6 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: ADP, MG Related: 3ez2, 3ez7, 3ez9, 3ezf Gene: parA ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PARA_ECOLX] This protein is essential for plasmid partition. It ensures the proper distribution of newly replicated plasmids to daughter cells during cell division. ParA is trans-acting. 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 The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfils a different function: DNA-binding transcription autoregulation. The structure of ParA is unknown as is how distinct nucleotides arbitrate its different functions. To address these questions, we carried out structural and biochemical studies. Crystal structures show that ParA consists of an elongated N-terminal alpha-helix, which unexpectedly mediates dimerization, a winged-HTH and a Walker-box containing C-domain. Biochemical data confirm that apoParA forms dimers at physiological concentrations. Comparisons of four apoParA structures reveal a strikingly flexible dimer interface that allows ParA to adopt multiple conformations. The ParA-ADP structure shows that ADP-binding activates DNA binding using a bipartite mechanism. First, it locks in one specific dimer conformation, and second, it induces the folding of two DNA-binding basic motifs that we show are critical for operator binding. Structural basis for ADP-mediated transcriptional regulation by P1 and P7 ParA.,Dunham TD, Xu W, Funnell BE, Schumacher MA EMBO J. 2009 Jun 17;28(12):1792-802. Epub 2009 May 21. PMID:19461582 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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