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PDBsum entry 2z43
Go to PDB code: 
protein Protein-protein interface(s) links
Recombination PDB id
2z43

 

 

 

 

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Contents
Protein chains
228 a.a. *
290 a.a. *
Waters ×1099
* Residue conservation analysis
PDB id:
2z43
Name: Recombination
Title: Structure of a twinned crystal of rada
Structure: DNA repair and recombination protein rada. Chain: a, b, c. Synonym: DNA strand exchange protein. Engineered: yes
Source: Sulfolobus solfataricus. Organism_taxid: 273057. Strain: p2. Gene: rada. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
1.93Å     R-factor:   0.191     R-free:   0.241
Authors: L.T.Chen,T.P.Ko,A.H.J.Wang,T.F.Wang
Key ref: L.T.Chen et al. (2007). Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein. Plos One, 2, e858. PubMed id: 17848989
Date:
12-Jun-07     Release date:   13-Nov-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q55075  (RADA_SULSO) -  DNA repair and recombination protein RadA from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc: 		324 a.a.
228 a.a.
Protein chains
Pfam   ArchSchema ?
Q55075  (RADA_SULSO) -  DNA repair and recombination protein RadA from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc: 		324 a.a.
290 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Plos One 2:e858 (2007)
PubMed id: 17848989  
 
 
Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein.
L.T.Chen, T.P.Ko, Y.W.Chang, K.A.Lin, A.H.Wang, T.F.Wang.
 
  ABSTRACT  
 
RecA family proteins engage in an ATP-dependent DNA strand exchange reaction that includes a ssDNA nucleoprotein helical filament and a homologous dsDNA sequence. In spite of more than 20 years of efforts, the molecular mechanism of homology pairing and strand exchange is still not fully understood. Here we report a crystal structure of Sulfolobus solfataricus RadA overwound right-handed filament with three monomers per helical pitch. This structure reveals conformational details of the first ssDNA binding disordered loop (denoted L1 motif) and the dsDNA binding N-terminal domain (NTD). L1 and NTD together form an outwardly open palm structure on the outer surface of the helical filament. Inside this palm structure, five conserved basic amino acid residues (K27, K60, R117, R223 and R229) surround a 25 A pocket that is wide enough to accommodate anionic ssDNA, dsDNA or both. Biochemical analyses demonstrate that these five positively charged residues are essential for DNA binding and for RadA-catalyzed D-loop formation. We suggest that the overwound right-handed RadA filament represents a functional conformation in the homology search and pairing reaction. A new structural model is proposed for the homologous interactions between a RadA-ssDNA nucleoprotein filament and its dsDNA target.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20062530 A.L.Okorokov, Y.L.Chaban, D.V.Bugreev, J.Hodgkinson, A.V.Mazin, and E.V.Orlova (2010).
Structure of the hDmc1-ssDNA filament reveals the principles of its architecture.
  PLoS One, 5, e8586.  
20308162 L.T.Chen, and A.H.Wang (2010).
A rationally designed peptide enhances homologous recombination in vitro and resistance to DNA damaging agents in vivo.
  Nucleic Acids Res, 38, 4361-4371.  
19338667 C.D.Lee, and T.F.Wang (2009).
The N-terminal domain of Escherichia coli RecA have multiple functions in promoting homologous recombination.
  J Biomed Sci, 16, 37.  
19642111 E.H.Egelman, and L.A.Amos (2009).
Electron microscopy of helical filaments: rediscovering buried treasures in negative stain.
  Bioessays, 31, 909-911.  
19295907 Y.W.Chang, T.P.Ko, C.D.Lee, Y.C.Chang, K.A.Lin, C.S.Chang, A.H.Wang, and T.F.Wang (2009).
Three new structures of left-handed RADA helical filaments: structural flexibility of N-terminal domain is critical for recombinase activity.
  PLoS ONE, 4, e4890.
PDB codes: 2zub 2zuc 2zud
18467498 C.D.Lee, H.C.Sun, S.M.Hu, C.F.Chiu, A.Homhuan, S.M.Liang, C.H.Leng, and T.F.Wang (2008).
An improved SUMO fusion protein system for effective production of native proteins.
  Protein Sci, 17, 1241-1248.  
18623074 E.H.Egelman (2008).
Helicity in electron microscopy images-a comment on Wang TF, Chen LT and Wang AH 2008 BioEssays 30:48-56.
  Bioessays, 30, 791-792.  
18937379 T.F.Wang, Y.C.Chang, C.D.Lee, L.Chen, C.S.Chang, and A.H.Wang (2008).
Authors' reply to correspondence from Egelman.
  Bioessays, 30, 1254-1255.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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