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Replication/DNA PDB id
1ecr
Jmol
Contents
Protein chain
305 a.a. *
DNA/RNA
Waters ×49
* Residue conservation analysis
PDB id:
1ecr
Name: Replication/DNA
Title: Escherichia coli replication terminator protein (tus) comple DNA
Structure: DNA (5'-d( Tp Tp Ap Gp Tp Tp Ap Cp Ap Ap Cp Ap Tp 3. Chain: b. Synonym: ter. Engineered: yes. DNA (5'-d( Tp Ap Gp Tp Ap Tp Gp Tp Tp Gp Tp Ap Ap 3. Chain: c. Synonym: ter.
Source: Synthetic: yes. Escherichia coli. Organism_taxid: 37762. Strain: b. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Hexamer (from PQS)
Resolution:
2.70Å     R-factor:   0.196     R-free:   0.314
Authors: K.Kamada,K.Morikawa
Key ref: K.Kamada et al. (1996). Structure of a replication-terminator protein complexed with DNA. Nature, 383, 598-603. PubMed id: 8857533 DOI: 10.1038/383598a0
Date:
01-Sep-96     Release date:   05-Sep-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16525  (TUS_ECOLI) -  DNA replication terminus site-binding protein
Seq:
Struc: 		309 a.a.
305 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     DNA replication   2 terms 
  Biochemical function     DNA binding     1 term  

 

 
DOI no: 10.1038/383598a0 Nature 383:598-603 (1996)
PubMed id: 8857533  
 
 
Structure of a replication-terminator protein complexed with DNA.
K.Kamada, T.Horiuchi, K.Ohsumi, N.Shimamoto, K.Morikawa.
 
  ABSTRACT  
 
The crystal structure of the Escherichia coli replication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 A resolution. The Tus protein folds into a previously undescribed architecture divided into two domains by a central basic cleft. This cleft accommodates locally deformed B-form Ter DNA and makes extensive contacts with the major groove, mainly through two interdomain beta-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20454718 M.J.Moreau, I.Morin, and P.M.Schaeffer (2010).
Quantitative determination of protein stability and ligand binding using a green fluorescent protein reporter system.
  Mol Biosyst, 6, 1285-1292.  
20126275 S.J.Kaczmarczyk, K.Sitaraman, T.Hill, J.L.Hartley, and D.K.Chatterjee (2010).
Tus, an E. coli protein, contains mammalian nuclear targeting and exporting signals.
  PLoS One, 5, e8889.  
19462083 D.B.Dahdah, I.Morin, M.J.Moreau, N.E.Dixon, and P.M.Schaeffer (2009).
Site-specific covalent attachment of DNA to proteins using a photoactivatable Tus-Ter complex.
  Chem Commun (Camb), 0, 3050-3052.  
19298368 D.L.Kaplan, and D.Bastia (2009).
Mechanisms of polar arrest of a replication fork.
  Mol Microbiol, 72, 279-285.  
19352501 I.Majumdar, L.N.Kinch, and N.V.Grishin (2009).
A database of domain definitions for proteins with complex interdomain geometry.
  PLoS ONE, 4, e5084.  
18708526 D.Bastia, S.Zzaman, G.Krings, M.Saxena, X.Peng, and M.M.Greenberg (2008).
Replication termination mechanism as revealed by Tus-mediated polar arrest of a sliding helicase.
  Proc Natl Acad Sci U S A, 105, 12831-12836.  
17347517 E.V.Mirkin, and S.M.Mirkin (2007).
Replication fork stalling at natural impediments.
  Microbiol Mol Biol Rev, 71, 13-35.  
16950091 D.L.Kaplan (2006).
Replication termination: mechanism of polar arrest revealed.
  Curr Biol, 16, R684-R686.  
16940176 G.Krings, and D.Bastia (2006).
Molecular architecture of a eukaryotic DNA replication terminus-terminator protein complex.
  Mol Cell Biol, 26, 8061-8074.  
16608433 J.L.Beck, T.Urathamakul, S.J.Watt, M.M.Sheil, P.M.Schaeffer, and N.E.Dixon (2006).
Proteomic dissection of DNA polymerization.
  Expert Rev Proteomics, 3, 197-211.  
  17077489 J.P.Vivian, C.Porter, J.A.Wilce, and M.C.Wilce (2006).
Crystallization and preliminary X-ray diffraction analysis of the Bacillus subtilis replication termination protein in complex with the 37-base-pair TerI-binding site.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1104-1107.  
16921356 K.Theis (2006).
One-way traffic control in replication termination.
  Nat Chem Biol, 2, 455-456.  
16814717 M.D.Mulcair, P.M.Schaeffer, A.J.Oakley, H.F.Cross, C.Neylon, T.M.Hill, and N.E.Dixon (2006).
A molecular mousetrap determines polarity of termination of DNA replication in E. coli.
  Cell, 125, 1309-1319.
PDB code: 2ewj
16148308 C.Neylon, A.V.Kralicek, T.M.Hill, and N.E.Dixon (2005).
Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex.
  Microbiol Mol Biol Rev, 69, 501-526.  
16238625 M.Valjavec-Gratian, T.A.Henderson, and T.M.Hill (2005).
Tus-mediated arrest of DNA replication in Escherichia coli is modulated by DNA supercoiling.
  Mol Microbiol, 58, 758-773.  
16211009 S.Bigot, O.A.Saleh, C.Lesterlin, C.Pages, M.El Karoui, C.Dennis, M.Grigoriev, J.F.Allemand, F.X.Barre, and F.Cornet (2005).
KOPS: DNA motifs that control E. coli chromosome segregation by orienting the FtsK translocase.
  EMBO J, 24, 3770-3780.  
15167891 O.A.Saleh, C.Pérals, F.X.Barre, and J.F.Allemand (2004).
Fast, DNA-sequence independent translocation by FtsK in a single-molecule experiment.
  EMBO J, 23, 2430-2439.  
15459336 R.Gupta, S.M.Hamdan, N.E.Dixon, M.M.Sheil, and J.L.Beck (2004).
Application of electrospray ionization mass spectrometry to study the hydrophobic interaction between the epsilon and theta subunits of DNA polymerase III.
  Protein Sci, 13, 2878-2887.  
15007108 R.Ohki, and F.Ishikawa (2004).
Telomere-bound TRF1 and TRF2 stall the replication fork at telomeric repeats.
  Nucleic Acids Res, 32, 1627-1637.  
15522074 S.Bigot, J.Corre, J.M.Louarn, F.Cornet, and F.X.Barre (2004).
FtsK activities in Xer recombination, DNA mobilization and cell division involve overlapping and separate domains of the protein.
  Mol Microbiol, 54, 876-886.  
11742131 A.Kapur, J.L.Beck, S.E.Brown, N.E.Dixon, and M.M.Sheil (2002).
Use of electrospray ionization mass spectrometry to study binding interactions between a replication terminator protein and DNA.
  Protein Sci, 11, 147-157.  
12097643 D.Kiga, K.Sakamoto, K.Kodama, T.Kigawa, T.Matsuda, T.Yabuki, M.Shirouzu, Y.Harada, H.Nakayama, K.Takio, Y.Hasegawa, Y.Endo, I.Hirao, and S.Yokoyama (2002).
An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system.
  Proc Natl Acad Sci U S A, 99, 9715-9720.  
12029035 T.Murata, M.Ohnishi, T.Ara, J.Kaneko, C.G.Han, Y.F.Li, K.Takashima, H.Nojima, K.Nakayama, A.Kaji, Y.Kamio, T.Miki, H.Mori, E.Ohtsubo, Y.Terawaki, and T.Hayashi (2002).
Complete nucleotide sequence of plasmid Rts1: implications for evolution of large plasmid genomes.
  J Bacteriol, 184, 3194-3202.  
11223520 J.P.Vivian, J.A.Wilce, A.F.Hastings, and M.C.Wilce (2001).
Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy.
  Acta Crystallogr D Biol Crystallogr, 57, 421-424.  
11168592 K.Namba (2001).
Roles of partly unfolded conformations in macromolecular self-assembly.
  Genes Cells, 6, 1.  
11493686 S.Mulugu, A.Potnis, Shamsuzzaman, J.Taylor, K.Alexander, and D.Bastia (2001).
Mechanism of termination of DNA replication of Escherichia coli involves helicase-contrahelicase interaction.
  Proc Natl Acad Sci U S A, 98, 9569-9574.  
10712935 J.L.Keck, and J.M.Berger (2000).
DNA replication at high resolution.
  Chem Biol, 7, R63-R71.  
  11104519 N.M.Luscombe, S.E.Austin, H.M.Berman, and J.M.Thornton (2000).
An overview of the structures of protein-DNA complexes.
  Genome Biol, 1, REVIEWS001.  
10931283 P.A.Andersen, A.A.Griffiths, I.G.Duggin, and R.G.Wake (2000).
Functional specificity of the replication fork-arrest complexes of Bacillus subtilis and Escherichia coli: significant specificity for Tus-Ter functioning in E. coli.
  Mol Microbiol, 36, 1327-1335.  
10209736 D.E.Bussiere, and D.Bastia (1999).
Termination of DNA replication of bacterial and plasmid chromosomes.
  Mol Microbiol, 31, 1611-1618.  
10026283 K.Nadassy, S.J.Wodak, and J.Janin (1999).
Structural features of protein-nucleic acid recognition sites.
  Biochemistry, 38, 1999-2017.  
9446621 B.K.Mohanty, T.Sahoo, and D.Bastia (1998).
Mechanistic studies on the impact of transcription on sequence-specific termination of DNA replication and vice versa.
  J Biol Chem, 273, 3051-3059.  
  9618448 G.del Solar, R.Giraldo, M.J.Ruiz-Echevarría, M.Espinosa, and R.Díaz-Orejas (1998).
Replication and control of circular bacterial plasmids.
  Microbiol Mol Biol Rev, 62, 434-464.  
9016600 A.V.Kralicek, P.K.Wilson, G.B.Ralston, R.G.Wake, and G.F.King (1997).
Reorganization of terminator DNA upon binding replication terminator protein: implications for the functional replication fork arrest complex.
  Nucleic Acids Res, 25, 590-596.  
9334221 F.F.Coskun-Ari, and T.M.Hill (1997).
Sequence-specific interactions in the Tus-Ter complex and the effect of base pair substitutions on arrest of DNA replication in Escherichia coli.
  J Biol Chem, 272, 26448-26456.  
9369480 K.J.Hacker, and K.A.Johnson (1997).
A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding.
  Biochemistry, 36, 14080-14087.  
9782775 M.Tateno, K.Yamasaki, N.Amano, J.Kakinuma, H.Koike, M.D.Allen, and M.Suzuki (1997).
DNA recognition by beta-sheets.
  Biopolymers, 44, 335-359.  
9271849 R.G.Wake (1997).
Replication fork arrest and termination of chromosome replication in Bacillus subtilis.
  FEMS Microbiol Lett, 153, 247-254.  
9033583 Y.Arata (1997).
Size is everything.
  Nat Struct Biol, 4, 93-94.  
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 code is shown on the right.