5DAC: Atp-gamma-s Bound Rad50 From Chaetomium Thermophilum In Complex With Dna

Citation:
Abstract
The Mre11-Rad50-Nbs1 (MRN) complex is a central factor in the repair ofDNAdouble-strand breaks (DSBs). TheATP-dependent mechanisms of howMRNdetects and endonucleolytically processesDNAends for the repair by microhomology-mediated end-joining or further resection in homologous recombination are still unclear. Here, we report the crystal structures of theATPgammaS-bound dimer of the Rad50(NBD)(nucleotide-binding domain) from the thermophilic eukaryoteChaetomium thermophilum(Ct) in complex with eitherDNAorCtMre11(RBD)(Rad50-binding domain) along with small-angle X-ray scattering and cross-linking studies. The structure andDNAbinding motifs were validated byDNAbinding experimentsin vitroand mutational analyses inSaccharomyces 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 ofDNAalong the dimer interface in anATP-dependent fashion or bridges two DNAends with a preference for 3' overhangs. Finally, our results may provide a general framework for the interaction ofABC ATPase domains of the Rad50/SMC/RecN protein family with DNA.
PDB ID: 5DACDownload
MMDB ID: 136996
PDB Deposition Date: 2015/8/19
Updated in MMDB: 2016/04
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Chaetomium thermophilum var. thermophilum DSM 1495
Similar Structures:
Biological Unit for 5DAC: tetrameric; determined by software (PISA)
Molecular Components in 5DAC
Label Count Molecule
Proteins (2 molecules)
2
Putative Uncharacterized Protein,putative Uncharacterized Protein
Molecule annotation
Nucleotides(2 molecules)
1
DNA (5'-d(p*cp*cp*cp*cp*cp*cp*cp*cp*cp*cp*cp*cp*cp*cp*c)- 3')
Molecule annotation
1
DNA (5'-d(p*gp*gp*gp*gp*gp*gp*gp*gp*gp*gp*gp*gp*gp*gp*g)- 3')
Molecule annotation
Chemicals (6 molecules)
1
2
2
2
3
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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