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1YUI

SOLUTION NMR STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX, REGULARIZED MEAN STRUCTURE

Summary for 1YUI
Entry DOI10.2210/pdb1yui/pdb
DescriptorDNA (5'-D(*GP*CP*CP*GP*AP*GP*AP*GP*TP*AP*C)-3'), DNA (5'-D(*GP*TP*AP*CP*TP*CP*TP*CP*GP*GP*C)-3'), GAGA-FACTOR, ... (4 entities in total)
Functional Keywordscomplex (dna-binding protein-dna), chromatin remodeling, dna binding protein-dna complex, dna binding protein/dna
Biological sourceDrosophila melanogaster (fruit fly)
Cellular locationNucleus: Q08605
Total number of polymer chains3
Total formula weight12976.04
Authors
Clore, G.M.,Omichinski, J.G.,Gronenborn, A.M. (deposition date: 1996-12-31, release date: 1997-12-31, Last modification date: 2024-05-22)
Primary citationOmichinski, J.G.,Pedone, P.V.,Felsenfeld, G.,Gronenborn, A.M.,Clore, G.M.
The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode.
Nat.Struct.Biol., 4:122-132, 1997
Cited by
PubMed Abstract: The structure of a complex between the DNA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magnetic resonance spectroscopy. The GAGA-DBD comprises a single classical Cys2-His2 zinc finger core, and an N-terminal extension containing two highly basic regions, BR1 and BR2. The zinc finger core binds in the major groove and recognizes the first three GAG bases of the consensus in a manner similar to that seen in other classical zinc finger-DNA complexes. Unlike the latter, which require tandem zinc finger repeats with a minimum of two units for high affinity binding, the GAGA-DBD makes use of only a single finger complemented by BR1 and BR2. BR2 forms a helix that interacts in the major groove recognizing the last G of the consensus, while BR1 wraps around the DNA in the minor groove and recognizes the A in the fourth position of the consensus. The implications of the structure of the GAGA-DBD-DNA complex for chromatin remodelling are discussed.
PubMed: 9033593
DOI: 10.1038/nsb0297-122
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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