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PDBsum entry 4cej

Go to PDB code: 
protein dna_rna ligands metals Protein-protein interface(s) links
Hydrolase/DNA PDB id
4cej
Jmol
Contents
Protein chains
1177 a.a.
1156 a.a.
DNA/RNA
Ligands
ANP ×2
SF4
Metals
_MG ×2
Waters ×7
PDB id:
4cej
Name: Hydrolase/DNA
Title: Crystal structure of addab-DNA-adpnp complex at 3 angstrom r
Structure: Atp-dependent helicase/nuclease subunit a. Chain: a. Synonym: atp-dependent helicase/nuclease adda. Engineered: yes. Mutation: yes. Atp-dependent helicase/deoxyribonuclease subunit chain: b. Synonym: atp-dependent helicase-nuclease subunit b, atp-dep helicase/nuclease addb.
Source: Bacillus subtilis subsp. Subtilis str. Organism_taxid: 224308. Atcc: 23857. Expressed in: escherichia coli b. Expression_system_taxid: 37762. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
Resolution:
3.00Å     R-factor:   0.204     R-free:   0.243
Authors: W.W.Krajewski,M.Wilkinson,X.Fu,N.B.Cronin,D.B.Wigley
Key ref: W.W.Krajewski et al. (2014). Structural basis for translocation by AddAB helicase-nuclease and its arrest at χ sites. Nature, 508, 416-419. PubMed id: 24670664 DOI: 10.1038/nature13037
Date:
11-Nov-13     Release date:   12-Mar-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P23478  (ADDA_BACSU) -  ATP-dependent helicase/nuclease subunit A
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1232 a.a.
1177 a.a.*
Protein chain
Pfam   ArchSchema ?
P23477  (ADDB_BACSU) -  ATP-dependent helicase/deoxyribonuclease subunit B
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1166 a.a.
1156 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.3.6.4.12  - Dna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate
ATP
+ H(2)O
=
ADP
Bound ligand (Het Group name = ANP)
matches with 81.25% similarity
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     nucleic acid phosphodiester bond hydrolysis   6 terms 
  Biochemical function     nucleotide binding     15 terms  

 

 
    reference    
 
 
DOI no: 10.1038/nature13037 Nature 508:416-419 (2014)
PubMed id: 24670664  
 
 
Structural basis for translocation by AddAB helicase-nuclease and its arrest at χ sites.
W.W.Krajewski, X.Fu, M.Wilkinson, N.B.Cronin, M.S.Dillingham, D.B.Wigley.
 
  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.