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2drp

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Revision as of 14:30, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 2drp

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, resolution 2.800Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

2DRP is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition., Fairall L, Schwabe JW, Chapman L, Finch JT, Rhodes D, Nature. 1993 Dec 2;366(6454):483-7. PMID:8247159

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