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PDBsum entry 2fdc

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protein dna_rna ligands links
DNA binding protein/DNA PDB id
2fdc

 

 

 

 

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Contents
Protein chains
505 a.a. *
585 a.a. *
DNA/RNA
Ligands
FLQ
* Residue conservation analysis
PDB id:
2fdc
Name: DNA binding protein/DNA
Title: Structural basis of DNA damage recognition and processing by uvrb: crystal structure of a uvrb/DNA complex
Structure: 5'-d(p Cp Gp Gp Cp Tp Cp Cp Ap Tp Cp Tp Cp Tp Ap Cp Cp Gp C p Ap A)-3'. Chain: c, d. Engineered: yes. Uvrabc system protein b. Chain: a, b. Synonym: uvrb protein, excinuclease abc subunit b. Engineered: yes
Source: Synthetic: yes. Bacillus caldotenax. Organism_taxid: 1395. Gene: uvrb. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
3.30Å     R-factor:   0.210     R-free:   0.258
Authors: J.J.Truglio,C.Kisker
Key ref:
J.J.Truglio et al. (2006). Structural basis for DNA recognition and processing by UvrB. Nat Struct Mol Biol, 13, 360-364. PubMed id: 16532007 DOI: 10.1038/nsmb1072
Date:
13-Dec-05     Release date:   14-Mar-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P56981  (UVRB_BACCA) -  UvrABC system protein B from Bacillus caldotenax
Seq:
Struc:
 
Seq:
Struc:
658 a.a.
505 a.a.
Protein chain
Pfam   ArchSchema ?
P56981  (UVRB_BACCA) -  UvrABC system protein B from Bacillus caldotenax
Seq:
Struc:
 
Seq:
Struc:
658 a.a.
585 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DNA/RNA chains
  C-G-G-C-T-T-A-C-C-G-C-A 12 bases
  C-C-G-C-A 5 bases

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1038/nsmb1072 Nat Struct Mol Biol 13:360-364 (2006)
PubMed id: 16532007  
 
 
Structural basis for DNA recognition and processing by UvrB.
J.J.Truglio, E.Karakas, B.Rhau, H.Wang, M.J.DellaVecchia, B.Van Houten, C.Kisker.
 
  ABSTRACT  
 
DNA-damage recognition in the nucleotide excision repair (NER) cascade is a complex process, operating on a wide variety of damages. UvrB is the central component in prokaryotic NER, directly involved in DNA-damage recognition and guiding the DNA through repair synthesis. We report the first structure of a UvrB-double-stranded DNA complex, providing insights into the mechanism by which UvrB binds DNA, leading to formation of the preincision complex. One DNA strand, containing a 3' overhang, threads behind a beta-hairpin motif of UvrB, indicating that this motif inserts between the strands of the double helix, thereby locking down either the damaged or undamaged strand. The nucleotide directly behind the beta-hairpin is flipped out and inserted into a small, highly conserved pocket in UvrB.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. The UvrB–DNA complex and selected electron density. (a) Surface of UvrB is color-coded by domain (yellow, 1a; green, 1b; blue, 2; red, 3; cyan, the -hairpin of UvrB; magenta, the newly formed -sheet after DNA binding). DNA is illustrated by spokes and letters, color-coded by nucleotide type. The letter representation of the DNA is in a similar orientation to the DNA in the structure. Black letters, disordered nucleotides; F, fluorescein-adducted thymine. The fluorescein-dT, although partially ordered (Fig. 1b), has been omitted from the figure for clarity. (b) 2F[o] - F[c] electron density map contoured at 1.0 covering the DNA. Gray, carbons of unmodified nucleotides; green, carbons of partially ordered fluorescein; magenta, electron density for the fluorescein. Nucleotides are labeled consecutively from 5' to 3', omitting numbers of disordered residues. (c) UvrB–DNA model showing how the inner strand of the DNA (red) travels between the -hairpin (cyan) and domain 1b and the outer strand (green) travels around the outside of the -hairpin. (d) Superposition of DNA-bound and apo UvrB. -hairpin regions of the DNA-bound (cyan and blue) and apo UvrB (PDB entry 1D9X; yellow and gold) are superimposed. Select residues are shown with color-coded labeling. Dark gray spokes represent the bound DNA and the surface of the remainder of the UvrB–DNA complex is shown in gray.
Figure 2.
Figure 2. Interactions between UvrB and the DNA. (a) UvrB bound to DNA. Gray surface, UvrB; cyan ribbon, -hairpin; yellow, outer DNA strand; green, inner DNA strand. Selected residues from UvrB are indicated. 3' and 5' ends of the DNA are labeled in red. Nucleotides are numbered sequentially starting from the 5' end and omitting numbers corresponding to nucleotides in the loop region. (b,c) Views rotated 45° (b) and 90° (c) from a along the vertical axis.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2006, 13, 360-364) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22307053 D.Pakotiprapha, M.Samuels, K.Shen, J.H.Hu, and D.Jeruzalmi (2012).
Structure and mechanism of the UvrA-UvrB DNA damage sensor.
  Nat Struct Mol Biol, 19, 291-298.
PDB codes: 3uwx 3ux8
21240268 M.Jaciuk, E.Nowak, K.Skowronek, A.TaƄska, and M.Nowotny (2011).
Structure of UvrA nucleotide excision repair protein in complex with modified DNA.
  Nat Struct Mol Biol, 18, 191-197.
PDB code: 3pih
21235228 N.Mazloum, M.A.Stegman, D.L.Croteau, B.Van Houten, N.S.Kwon, Y.Ling, C.Dickinson, A.Venugopal, M.A.Towheed, and C.Nathan (2011).
Identification of a chemical that inhibits the mycobacterial UvrABC complex in nucleotide excision repair.
  Biochemistry, 50, 1329-1335.  
20386832 K.Isozaki, and K.Miki (2010).
Design, synthesis, and complementary recognition of beta-hairpin peptides stabilized by artificial DNA base-pairing amino acids.
  Chem Commun (Camb), 46, 2947-2949.  
21145481 L.Manelyte, Y.I.Kim, A.J.Smith, R.M.Smith, and N.J.Savery (2010).
Regulation and rate enhancement during transcription-coupled DNA repair.
  Mol Cell, 40, 714-724.  
20227373 N.M.Kad, H.Wang, G.G.Kennedy, D.M.Warshaw, and B.Van Houten (2010).
Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins.
  Mol Cell, 37, 702-713.  
19287003 D.Pakotiprapha, Y.Liu, G.L.Verdine, and D.Jeruzalmi (2009).
A Structural Model for the Damage-sensing Complex in Bacterial Nucleotide Excision Repair.
  J Biol Chem, 284, 12837-12844.
PDB code: 3fpn
19549864 H.Wang, M.Lu, M.S.Tang, B.Van Houten, J.B.Ross, M.Weinfeld, and X.C.Le (2009).
DNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway.
  Proc Natl Acad Sci U S A, 106, 12849-12854.  
19208629 J.Atkinson, C.P.Guy, C.J.Cadman, G.F.Moolenaar, N.Goosen, and P.McGlynn (2009).
Stimulation of UvrD helicase by UvrAB.
  J Biol Chem, 284, 9612-9623.  
19208636 K.Wagner, G.Moolenaar, J.van Noort, and N.Goosen (2009).
Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer.
  Nucleic Acids Res, 37, 1962-1972.  
19681599 L.Jia, K.Kropachev, S.Ding, B.Van Houten, N.E.Geacintov, and S.Broyde (2009).
Exploring damage recognition models in prokaryotic nucleotide excision repair with a benzo[a]pyrene-derived lesion in UvrB.
  Biochemistry, 48, 8948-8957.  
19762288 L.Manelyte, C.P.Guy, R.M.Smith, M.S.Dillingham, P.McGlynn, and N.J.Savery (2009).
The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair.
  DNA Repair (Amst), 8, 1300-1310.  
18248777 D.L.Croteau, M.J.DellaVecchia, L.Perera, and B.Van Houten (2008).
Cooperative damage recognition by UvrA and UvrB: identification of UvrA residues that mediate DNA binding.
  DNA Repair (Amst), 7, 392-404.  
18158267 D.Pakotiprapha, Y.Inuzuka, B.R.Bowman, G.F.Moolenaar, N.Goosen, D.Jeruzalmi, and G.L.Verdine (2008).
Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding.
  Mol Cell, 29, 122-133.
PDB code: 2r6f
18329872 E.J.Enemark, and L.Joshua-Tor (2008).
On helicases and other motor proteins.
  Curr Opin Struct Biol, 18, 243-257.  
18996898 L.A.Christensen, H.Wang, B.Van Houten, and K.M.Vasquez (2008).
Efficient processing of TFO-directed psoralen DNA interstrand crosslinks by the UvrABC nuclease.
  Nucleic Acids Res, 36, 7136-7145.  
18166981 S.C.Shuck, E.A.Short, and J.J.Turchi (2008).
Eukaryotic nucleotide excision repair: from understanding mechanisms to influencing biology.
  Cell Res, 18, 64-72.  
18578568 S.C.Wolski, J.Kuper, P.Hänzelmann, J.J.Truglio, D.L.Croteau, B.Van Houten, and C.Kisker (2008).
Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD.
  PLoS Biol, 6, e149.
PDB code: 2vsf
18157156 W.Yang (2008).
Structure and mechanism for DNA lesion recognition.
  Cell Res, 18, 184-197.  
17245438 E.Karakas, J.J.Truglio, D.Croteau, B.Rhau, L.Wang, B.Van Houten, and C.Kisker (2007).
Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.
  EMBO J, 26, 613-622.
PDB codes: 2nrr 2nrt 2nrv 2nrw 2nrx 2nrz
17822711 M.J.DellaVecchia, W.K.Merritt, Y.Peng, T.W.Kirby, E.F.DeRose, G.A.Mueller, B.Van Houten, and R.E.London (2007).
NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution.
  J Mol Biol, 373, 282-295.  
17572090 N.J.Savery (2007).
The molecular mechanism of transcription-coupled DNA repair.
  Trends Microbiol, 15, 326-333.  
17962020 O.Maillard, U.Camenisch, F.C.Clement, K.B.Blagoev, and H.Naegeli (2007).
DNA repair triggered by sensors of helical dynamics.
  Trends Biochem Sci, 32, 494-499.  
17525736 S.Karamanou, G.Gouridis, E.Papanikou, G.Sianidis, I.Gelis, D.Keramisanou, E.Vrontou, C.G.Kalodimos, and A.Economou (2007).
Preprotein-controlled catalysis in the helicase motor of SecA.
  EMBO J, 26, 2904-2914.  
16595666 H.Wang, M.J.DellaVecchia, M.Skorvaga, D.L.Croteau, D.A.Erie, and B.Van Houten (2006).
UvrB domain 4, an autoinhibitory gate for regulation of DNA binding and ATPase activity.
  J Biol Chem, 281, 15227-15237.  
16973432 J.Rudolf, V.Makrantoni, W.J.Ingledew, M.J.Stark, and M.F.White (2006).
The DNA repair helicases XPD and FancJ have essential iron-sulfur domains.
  Mol Cell, 23, 801-808.  
16921356 K.Theis (2006).
One-way traffic control in replication termination.
  Nat Chem Biol, 2, 455-456.  
17145708 R.Gupta, S.Sharma, K.M.Doherty, J.A.Sommers, S.B.Cantor, and R.M.Brosh (2006).
Inhibition of BACH1 (FANCJ) helicase by backbone discontinuity is overcome by increased motor ATPase or length of loading strand.
  Nucleic Acids Res, 34, 6673-6683.  
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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