2DRP

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

Summary for 2DRP

• Entry DOI: 10.2210/pdb2drp/pdb
• Descriptor: DNA (5'-D(*CP*TP*AP*AP*TP*AP*AP*GP*GP*AP*TP*AP*AP*CP*GP*TP*C P*CP*G)-3'), DNA (5'-D(*TP*CP*GP*GP*AP*CP*GP*TP*TP*AP*TP*CP*CP*TP*TP*AP*T P*TP*A)-3'), PROTEIN (TRAMTRACK DNA-BINDING DOMAIN), ... (5 entities in total)
• Functional Keywords: protein-dna complex, double helix, transcription-dna complex, transcription/dna
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Nucleus: P17789
• Total number of polymer chains: 6
• Total formula weight: 39597.69

Authors

Fairall, L.,Schwabe, J.W.R.,Chapman, L.,Finch, J.T.,Rhodes, D. (deposition date: 1994-06-06, release date: 1994-08-31, Last modification date: 2024-02-14)

Primary citation

Fairall, L.,Schwabe, J.W.,Chapman, L.,Finch, J.T.,Rhodes, D.
The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition.
Nature, 366:483-487, 1993

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.

PubMed: 8247159
DOI: 10.1038/366483a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)