2DRP

THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Work: 0.193 
  • R-Value Observed: 0.193 

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This is version 1.3 of the entry. See complete history. 


Literature

The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition.

Fairall, L., Schwabe, J.W., Chapman, L., Finch, J.T., Rhodes, D.

(1993) Nature 366: 483-487

  • DOI: https://doi.org/10.1038/366483a0
  • Primary Citation of Related Structures:  
    2DRP

  • PubMed Abstract: 

    The Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition suggesting that the zinc-finger might represent a candidate template for designing proteins to recognize DNA. Residues at three key positions in an alpha-helical 'reading head' play a dominant role in base-recognition and have been targets for mutagenesis experiments aimed at deriving a recognition code. Here we report the structure of a two zinc-finger DNA-binding domain from the protein Tramtrack complexed with DNA. The amino-terminal zinc-finger and its interaction with DNA illustrate several novel features. These include the use of a serine residue, which is semi-conserved and located outside the three key positions, to make a base contact. Its role in base-recognition correlates with a large, local, protein-induced deformation of the DNA helix at a flexible A-T-A sequence and may give insight into previous mutagenesis experiments. It is apparent from this structure that zinc-finger/DNA recognition is more complex than was originally perceived.

    • Organizational Affiliation: 

    MRC Laboratory of Molecular Biology, Cambridge, UK.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (TRAMTRACK DNA-BINDING DOMAIN)E [auth A],
F [auth D]		66Drosophila melanogasterMutation(s): 0 
UniProt
Find proteins for P17789 (Drosophila melanogaster)
Explore P17789 
Go to UniProtKB:  P17789
Entity Groups  
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UniProt GroupP17789
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
DNA (5'-D(*CP*TP*AP*AP*TP*AP*AP*GP*GP*AP*TP*AP*AP*CP*GP*TP*C P*CP*G)-3')A [auth B],
C [auth E]		19N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-D(*TP*CP*GP*GP*AP*CP*GP*TP*TP*AP*TP*CP*CP*TP*TP*AP*T P*TP*A)-3')B [auth C],
D [auth F]		19N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Work: 0.193 
  • R-Value Observed: 0.193 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.7α = 90
b = 64.6β = 90
c = 117.6γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1994-08-31
    Type: Initial release
  • Version 1.1: 2008-05-22
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Derived calculations