4NOE
Crystal structure of DdrB bound to 30b ssDNA
Summary for 4NOE
| Entry DOI | 10.2210/pdb4noe/pdb |
| Descriptor | Single-stranded DNA-binding protein DdrB, 5'-D(*TP*TP*GP*CP*GP*CP*TP*TP*GP*CP*GP*CP*TP*TP*GP*CP*GP*CP*TP*TP*GP*CP*GP*CP*TP*TP*GP*CP*GP*CP)-3', CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | single-stranded dna annealing, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Deinococcus radiodurans |
| Total number of polymer chains | 6 |
| Total formula weight | 93861.17 |
| Authors | Sugiman-Marangos, S.N.,Weiss, Y.M.,Junop, M.S. (deposition date: 2013-11-19, release date: 2015-05-20, Last modification date: 2023-09-20) |
| Primary citation | Sugiman-Marangos, S.N.,Weiss, Y.M.,Junop, M.S. Mechanism for accurate, protein-assisted DNA annealing by Deinococcus radiodurans DdrB. Proc.Natl.Acad.Sci.USA, 113:4308-4313, 2016 Cited by PubMed Abstract: Accurate pairing of DNA strands is essential for repair of DNA double-strand breaks (DSBs). How cells achieve accurate annealing when large regions of single-strand DNA are unpaired has remained unclear despite many efforts focused on understanding proteins, which mediate this process. Here we report the crystal structure of a single-strand annealing protein [DdrB (DNA damage response B)] in complex with a partially annealed DNA intermediate to 2.2 Å. This structure and supporting biochemical data reveal a mechanism for accurate annealing involving DdrB-mediated proofreading of strand complementarity. DdrB promotes high-fidelity annealing by constraining specific bases from unauthorized association and only releases annealed duplex when bound strands are fully complementary. To our knowledge, this mechanism provides the first understanding for how cells achieve accurate, protein-assisted strand annealing under biological conditions that would otherwise favor misannealing. PubMed: 27044084DOI: 10.1073/pnas.1520847113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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