2DGC

GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA

Summary for 2DGC

• Entry DOI: 10.2210/pdb2dgc/pdb
• Related: 1DGC
• Descriptor: DNA (5'-D(*TP*GP*GP*AP*GP*AP*TP*GP*AP*CP*GP*TP*CP*AP*TP*CP*T P*CP*C)-3'), PROTEIN (GCN4) (3 entities in total)
• Functional Keywords: basic domain, leucine zipper, dna binding, eukaryotic regulatory protein, transcription-dna complex, transcription/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 2
• Total formula weight: 13196.33

Authors

Keller, W.,Koenig, P.,Richmond, T.J. (deposition date: 1995-09-28, release date: 1996-03-08, Last modification date: 2024-02-14)

Primary citation

Keller, W.,Konig, P.,Richmond, T.J.
Crystal structure of a bZIP/DNA complex at 2.2 A: determinants of DNA specific recognition.
J.Mol.Biol., 254:657-667, 1995

PubMed Abstract: The X-ray structure of the GCN4-bZIP protein bound to DNA containing the ATF/CREB recognition sequence has been refined at 2.2 A. The water-mediated interactions between the basic domain and DNA are revealed, and combined with a more accurate description of the direct contacts, further clarify how binding specificity is achieved. Water molecules extend the interactions of both invariant basic domain residues, asparagine 235 and arginine 243, beyond their direct base contacts. The slight bending of the basic domain alpha-helix around the DNA facilitates the linking of arginine 241, 243 and 245 to main-chain carbonyl oxygen atoms via water molecules, apparently stabilizing interactions with the DNA.

PubMed: 7500340
DOI: 10.1006/jmbi.1995.0645

Experimental method

X-RAY DIFFRACTION (2.2 Å)