4gat
From Proteopedia
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SOLUTION NMR STRUCTURE OF THE WILD TYPE DNA BINDING DOMAIN OF AREA COMPLEXED TO A 13BP DNA CONTAINING A CGATA SITE, REGULARIZED MEAN STRUCTURE
Overview
The solution structure of a complex between the DNA binding domain of a, fungal GATA factor and a 13 base-pair oligonucleotide containing its, physiologically relevant CGATAG target sequence has been determined by, multidimensional nuclear magnetic resonance spectroscopy. The AREA DNA, binding domain, from Aspergillus nidulans, possesses a single Cys2-Cys2, zinc finger module and a basic C-terminal tail, which recognize the CGATAG, element via an extensive network of hydrophobic interactions with the, bases in the major groove and numerous non-specific contacts along the, sugar-phosphate backbone. The zinc finger core of the AREA DNA binding, domain has the same global fold as that of the C-terminal DNA binding, domain of chicken GATA-1. In contrast to the complex with the DNA binding, domain of GATA-1 in which the basic C-terminal tail wraps around the DNA, and lies in the minor groove, the structure of complex with the AREA DNA, binding domain reveals that the C-terminal tail of the fungal domain runs, parallel with the sugar phosphate backbone along the edge of the minor, groove. This difference is principally attributed to amino acid, substitutions at two positions of the AREA DNA binding domain (Val55, Asn62) relative to that of GATA-1 (Gly55, Lys62). The impact of the, different C-terminal tail binding modes on the affinity and specificity of, GATA factors is discussed.
About this Structure
4GAT is a Single protein structure of sequence from Emericella nidulans with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The solution structure of a fungal AREA protein-DNA complex: an alternative binding mode for the basic carboxyl tail of GATA factors., Starich MR, Wikstrom M, Arst HN Jr, Clore GM, Gronenborn AM, J Mol Biol. 1998 Apr 3;277(3):605-20. PMID:9533883
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