4CEH
Crystal structure of AddAB with a forked DNA substrate
Summary for 4CEH
Entry DOI | 10.2210/pdb4ceh/pdb |
Related | 4CEI 4CEJ |
Descriptor | ATP-DEPENDENT HELICASE/NUCLEASE SUBUNIT A, ATP-DEPENDENT HELICASE/DEOXYRIBONUCLEASE SUBUNIT B, DNA, ... (4 entities in total) |
Functional Keywords | hydrolase-dna complex, helicase-nuclease, bacterial proteins, binding sites, dna breaks, double-stranded, dna helicases, dna repair, dna- binding proteins, exodeoxyribonuclease v, exodeoxyribonucleases, homologous recombination, hydrolase/dna |
Biological source | BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168 More |
Total number of polymer chains | 3 |
Total formula weight | 296296.63 |
Authors | Krajewski, W.W.,Wilkinson, M.,Fu, X.,Cronin, N.B.,Wigley, D. (deposition date: 2013-11-11, release date: 2014-03-12, Last modification date: 2023-12-20) |
Primary citation | Krajewski, W.W.,Fu, X.,Wilkinson, M.,Cronin, N.B.,Dillingham, M.S.,Wigley, D.B. Structural Basis for Translocation by Addab Helicase-Nuclease and its Arrest at Chi Sites. Nature, 508:416-, 2014 Cited by PubMed Abstract: In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is dependent upon the recombination hotspot sequence χ (Chi) and is catalysed by either an AddAB- or RecBCD-type helicase-nuclease (reviewed in refs 3, 4). These enzyme complexes unwind and digest the DNA duplex from the broken end until they encounter a χ sequence, whereupon they produce a 3' single-stranded DNA tail onto which they initiate loading of the RecA protein. Consequently, regulation of the AddAB/RecBCD complex by χ is a key control point in DNA repair and other processes involving genetic recombination. Here we report crystal structures of Bacillus subtilis AddAB in complex with different χ-containing DNA substrates either with or without a non-hydrolysable ATP analogue. Comparison of these structures suggests a mechanism for DNA translocation and unwinding, suggests how the enzyme binds specifically to χ sequences, and explains how χ recognition leads to the arrest of AddAB (and RecBCD) translocation that is observed in single-molecule experiments. PubMed: 24670664DOI: 10.1038/NATURE13037 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.24 Å) |
Structure validation
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