5dac

ATP-gamma-S bound Rad50 from Chaetomium thermophilum in complex with DNA

spinqualitylabelsall models 5dac, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dac is a 4 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.503Å Ligands: AES, AGS, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0SHW7_CHATD Publication Abstract from PubMed The Mre11-Rad50-Nbs1 (MRN) complex is a central factor in the repair of DNA double-strand breaks (DSBs). The ATP-dependent mechanisms of how MRN detects and endonucleolytically processes DNA ends for the repair by microhomology-mediated end-joining or further resection in homologous recombination are still unclear. Here, we report the crystal structures of the ATPgammaS-bound dimer of the Rad50NBD (nucleotide-binding domain) from the thermophilic eukaryote Chaetomium thermophilum (Ct) in complex with either DNA or CtMre11RBD (Rad50-binding domain) along with small-angle X-ray scattering and cross-linking studies. The structure and DNA binding motifs were validated by DNA binding experiments in vitro and mutational analyses in Saccharomyces cerevisiae in vivo. Our analyses provide a structural framework for the architecture of the eukaryotic Mre11-Rad50 complex. They show that a Rad50 dimer binds approximately 18 base pairs of DNA along the dimer interface in an ATP-dependent fashion or bridges two DNA ends with a preference for 3' overhangs. Finally, our results may provide a general framework for the interaction of ABC ATPase domains of the Rad50/SMC/RecN protein family with DNA. Structural mechanism of ATP-dependent DNA binding and DNA end bridging by eukaryotic Rad50.,Seifert FU, Lammens K, Stoehr G, Kessler B, Hopfner KP EMBO J. 2016 Feb 19. pii: e201592934. PMID:26896444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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