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PDBsum entry 4hqb

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protein dna_rna Protein-protein interface(s) links
DNA binding protein/DNA PDB id
4hqb

 

 

 

 

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Contents
Protein chains
143 a.a.
131 a.a.
118 a.a.
109 a.a.
128 a.a.
DNA/RNA
Waters ×199
PDB id:
4hqb
Name: DNA binding protein/DNA
Title: Crystal structure of ddrb from deinococcus radiodurans bound to ssdna
Structure: Single-stranded DNA-binding protein ddrb. Chain: a, b, c, d, e. Synonym: DNA damage response protein b. Engineered: yes. 5'-d( Tp Tp Tp T)-3'. Chain: m. Engineered: yes. 5'-d(p Tp Tp Tp Tp T)-3'. Chain: n.
Source: Deinococcus radiodurans. Organism_taxid: 1299. Gene: ddrb, ddrb (dr0070), dr_0070. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Synthetic: yes
Resolution:
2.30Å     R-factor:   0.193     R-free:   0.246
Authors: S.N.Sugiman-Marangos,M.S.Junop
Key ref: S.N.Sugiman-Marangos et al. (2013). Crystal structure of the DdrB/ssDNA complex from Deinococcus radiodurans reveals a DNA binding surface involving higher-order oligomeric states. Nucleic Acids Res, 41, 9934-9944. PubMed id: 23975200 DOI: 10.1093/nar/gkt759
Date:
25-Oct-12     Release date:   04-Sep-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9RY80  (DDRB_DEIRA) -  Single-stranded DNA-binding protein DdrB from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Seq:
Struc:
188 a.a.
143 a.a.
Protein chain
Pfam   ArchSchema ?
Q9RY80  (DDRB_DEIRA) -  Single-stranded DNA-binding protein DdrB from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Seq:
Struc:
188 a.a.
131 a.a.
Protein chain
Pfam   ArchSchema ?
Q9RY80  (DDRB_DEIRA) -  Single-stranded DNA-binding protein DdrB from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Seq:
Struc:
188 a.a.
118 a.a.
Protein chain
Pfam   ArchSchema ?
Q9RY80  (DDRB_DEIRA) -  Single-stranded DNA-binding protein DdrB from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Seq:
Struc:
188 a.a.
109 a.a.
Protein chain
Pfam   ArchSchema ?
Q9RY80  (DDRB_DEIRA) -  Single-stranded DNA-binding protein DdrB from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Seq:
Struc:
188 a.a.
128 a.a.
Key:    PfamA domain  Secondary structure

DNA/RNA chains
  T-T-T-T 4 bases
  T-T-T-T-T 5 bases

 

 
DOI no: 10.1093/nar/gkt759 Nucleic Acids Res 41:9934-9944 (2013)
PubMed id: 23975200  
 
 
Crystal structure of the DdrB/ssDNA complex from Deinococcus radiodurans reveals a DNA binding surface involving higher-order oligomeric states.
S.N.Sugiman-Marangos, J.K.Peel, Y.M.Weiss, R.Ghirlando, M.S.Junop.
 
  ABSTRACT  
 
The ability of Deinococcus radiodurans to recover from extensive DNA damage is due in part to its ability to efficiently repair its genome, even following severe fragmentation by hundreds of double-strand breaks. The single-strand annealing pathway plays an important role early during the recovery process, making use of a protein, DdrB, shown to greatly stimulate ssDNA annealing. Here, we report the structure of DdrB bound to ssDNA to 2.3 Å. Pentameric DdrB was found to assemble into higher-order structures that coat ssDNA. To gain further mechanistic insight into the protein's function, a number of point mutants were generated altering both DNA binding and higher order oligomerization. This work not only identifies higher-order DdrB associations but also suggests the presence of an extended DNA binding surface running along the 'top' surface of a DdrB pentamer and continuing down between two individual subunits of the ring structure. Together this work sheds new insight into possible mechanisms for DdrB function in which higher-order assemblies of DdrB pentamers assist in the pairing of complementary ssDNA using an extended DNA binding surface.
 

 

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