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PDBsum entry 3e1s

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Hydrolase PDB id
3e1s

 

 

 

 

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Contents
Protein chain
517 a.a. *
Waters ×265
* Residue conservation analysis
PDB id:
3e1s
Name: Hydrolase
Title: Structure of an n-terminal truncation of deinococcus radiodurans recd2
Structure: Exodeoxyribonuclease v, subunit recd. Chain: a. Fragment: n-terminus deletion mutant of recd2, unp residues 151-715. Engineered: yes
Source: Deinococcus radiodurans. Organism_taxid: 1299. Gene: recd. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.235     R-free:   0.287
Authors: K.Saikrishnan,S.P.Griffiths,N.Cook,R.Court,D.B.Wigley
Key ref: K.Saikrishnan et al. (2008). DNA binding to RecD: role of the 1B domain in SF1B helicase activity. Embo J, 27, 2222-2229. PubMed id: 18668125
Date:
04-Aug-08     Release date:   19-Aug-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9RT63  (RECDL_DEIRA) -  ATP-dependent RecD2 DNA helicase from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Seq:
Struc:
 
Seq:
Struc:
715 a.a.
517 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.6.2.3  - Dna 5'-3' helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Embo J 27:2222-2229 (2008)
PubMed id: 18668125  
 
 
DNA binding to RecD: role of the 1B domain in SF1B helicase activity.
K.Saikrishnan, S.P.Griffiths, N.Cook, R.Court, D.B.Wigley.
 
  ABSTRACT  
 
The molecular mechanism of superfamily 1Balpha helicases remains unclear. We present here the crystal structure of the RecD2 helicase from Deinococcus radiodurans at 2.2-A resolution. The structure reveals the folds of the 1B and 2B domains of RecD that were poorly ordered in the structure of the Escherichia coli RecBCD enzyme complex reported previously. The 2B domain adopts an SH3 fold which, although common in eukaryotes, is extremely rare in bacterial systems. In addition, the D. radiodurans RecD2 structure has aided us in deciphering lower resolution (3.6 A) electron density maps for the E. coli RecBCD enzyme in complex with a long DNA substrate that interacts with the RecD subunit. Taken together, these structures indicated an important role for the 1B domain of RecD, a beta-hairpin that extends from the surface of the 1A domain and interacts with the DNA substrate. On the basis of these structural data, we designed a mutant RecD2 helicase that lacks this pin. The 'pin-less' mutant protein is a fully active ssDNA-dependent ATPase but totally lacks helicase activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23202527 D.B.Wigley (2012).
Bacterial DNA repair: recent insights into the mechanism of RecBCD, AddAB and AdnAB.
  Nat Rev Microbiol, 11, 9.  
20852646 C.G.Wu, C.Bradford, and T.M.Lohman (2010).
Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor.
  Nat Struct Mol Biol, 17, 1210-1217.  
20435720 L.Dostál, and J.F.Schildbach (2010).
Single-stranded DNA binding by F TraI relaxase and helicase domains is coordinately regulated.
  J Bacteriol, 192, 3620-3628.  
19920138 M.C.Unciuleac, and S.Shuman (2010).
Characterization of the mycobacterial AdnAB DNA motor provides insights into the evolution of bacterial motor-nuclease machines.
  J Biol Chem, 285, 2632-2641.  
21143323 S.Lang, K.Gruber, S.Mihajlovic, R.Arnold, C.J.Gruber, S.Steinlechner, M.A.Jehl, T.Rattei, K.U.Fröhlich, and E.L.Zechner (2010).
Molecular recognition determinants for type IV secretion of diverse families of conjugative relaxases.
  Mol Microbiol, 78, 1539-1555.  
19256528 L.P.Blair, A.J.Tackett, and K.D.Raney (2009).
Development and evaluation of a structural model for SF1B helicase Dda.
  Biochemistry, 48, 2321-2329.  
19946136 M.L.Bochman, and A.Schwacha (2009).
The Mcm complex: unwinding the mechanism of a replicative helicase.
  Microbiol Mol Biol Rev, 73, 652-683.  
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.

 

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