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PDBsum entry 1olo

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protein ligands Protein-protein interface(s) links
Transcription PDB id
1olo
Jmol
Contents
Protein chains
249 a.a. *
Ligands
SO4 ×2
Waters ×421
* Residue conservation analysis
PDB id:
1olo
Name: Transcription
Title: Hexameric replicative DNA helicase repa from plasmid rsf1010 - cubic crystal structure
Structure: Regulatory protein repa. Chain: a, b. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: broad host range plasmid rsf1010
Biol. unit: Hexamer (from PDB file)
Resolution:
2.55Å     R-factor:   0.176     R-free:   0.211
Authors: T.Niedenzu,W.Saenger
Key ref: G.Ziegelin et al. (2003). Hexameric RSF1010 helicase RepA: the structural and functional importance of single amino acid residues. Nucleic Acids Res, 31, 5917-5929. PubMed id: 14530440 DOI: 10.1093/nar/gkg790
Date:
08-Aug-03     Release date:   19-Sep-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P20356  (REPJ_ECOLX) -  Regulatory protein RepA
Seq:
Struc:
279 a.a.
249 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     nucleotide binding     3 terms  

 

 
DOI no: 10.1093/nar/gkg790 Nucleic Acids Res 31:5917-5929 (2003)
PubMed id: 14530440  
 
 
Hexameric RSF1010 helicase RepA: the structural and functional importance of single amino acid residues.
G.Ziegelin, T.Niedenzu, R.Lurz, W.Saenger, E.Lanka.
 
  ABSTRACT  
 
In the known monoclinic crystals the 3-dimensional structure of the hexameric, replicative helicase RepA encoded by plasmid RSF1010 shows 6-fold rotational symmetry. In contrast, in the cubic crystal form at 2.55 A resolution described here RepA has 3-fold symmetry and consists of a trimer of dimers. To study structure-function relationships, a series of repA deletion mutants and mutations yielding single amino acid exchanges were constructed and the respective gene products were analyzed in vivo and in vitro. Hexamerization of RepA occurs via the N-terminus and is required for NTP hydrolysis. The C-terminus is essential both for the interaction with the replication machinery and for the helicase activity. Functional analyses of RepA variants with single amino acid exchanges confirmed most of the predictions that were based on the published 3-dimensional structure. Of the five motifs conserved in family 4 helicases, all residues conserved in RepA and T7 gp4 helicases participate in DNA unwinding. Residues K42, E76, D77, D139 and H178, proposed to play key roles in catalyzing the hydrolysis of NTPs, are essential for RepA activity. Residue H178 of motif H3 couples nucleotide consumption to DNA strand separation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18647240 N.D.Thomsen, and J.M.Berger (2008).
Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases.
  Mol Microbiol, 69, 1071-1090.  
18593709 Y.Matsushima, C.L.Farr, L.Fan, and L.S.Kaguni (2008).
Physiological and biochemical defects in carboxyl-terminal mutants of mitochondrial DNA helicase.
  J Biol Chem, 283, 23964-23971.  
17722119 E.Sarzi, S.Goffart, V.Serre, D.Chrétien, A.Slama, A.Munnich, J.N.Spelbrink, and A.Rötig (2007).
Twinkle helicase (PEO1) gene mutation causes mitochondrial DNA depletion.
  Ann Neurol, 62, 579-587.  
16427007 D.J.Crampton, S.Mukherjee, and C.C.Richardson (2006).
DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase.
  Mol Cell, 21, 165-174.  
16935874 J.B.Boulé, and V.A.Zakian (2006).
Roles of Pif1-like helicases in the maintenance of genomic stability.
  Nucleic Acids Res, 34, 4147-4153.  
15579680 J.B.Bessler, and V.A.Zakian (2004).
The amino terminus of the Saccharomyces cerevisiae DNA helicase Rrm3p modulates protein function altering replication and checkpoint activity.
  Genetics, 168, 1205-1218.  
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.