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4CEJ

Crystal structure of AddAB-DNA-ADPNP complex at 3 Angstrom resolution

Summary for 4CEJ
Entry DOI10.2210/pdb4cej/pdb
Related4CEH 4CEI
DescriptorATP-DEPENDENT HELICASE/NUCLEASE SUBUNIT A, ATP-DEPENDENT HELICASE/DEOXYRIBONUCLEASE SUBUNIT B, DNA, ... (7 entities in total)
Functional Keywordshydrolase-dna complex, helicase-nuclease, dna breaks, dna repair, single-stranded, dna-binding proteins, exodeoxyribonuclease v, exodeoxyribonucleases, homologous recombination, hydrolase/dna
Biological sourceBACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168
More
Total number of polymer chains3
Total formula weight298878.59
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 citationKrajewski, 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: 24670664
DOI: 10.1038/NATURE13037
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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