1GD2

CRYSTAL STRUCTURE OF BZIP TRANSCRIPTION FACTOR PAP1 BOUND TO DNA

Summary for 1GD2

• Entry DOI: 10.2210/pdb1gd2/pdb
• Descriptor: DNA (5'-D(*AP*GP*GP*TP*TP*AP*CP*GP*TP*AP*AP*CP*C)-3'), TRANSCRIPTION FACTOR PAP1 (3 entities in total)
• Functional Keywords: basic leucine zipper, protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Cellular location: Cytoplasm: Q01663
• Total number of polymer chains: 10
• Total formula weight: 66047.47

Authors

Fujii, Y.,Shimizu, T.,Toda, T.,Yanagida, M.,Hakoshima, T. (deposition date: 2000-08-25, release date: 2000-10-02, Last modification date: 2023-12-27)

Primary citation

Fujii, Y.,Shimizu, T.,Toda, T.,Yanagida, M.,Hakoshima, T.
Structural basis for the diversity of DNA recognition by bZIP transcription factors.
Nat.Struct.Biol., 7:889-893, 2000

PubMed Abstract: The basic region leucine zipper (bZIP) proteins form one of the largest families of transcription factors in eukaryotic cells. Despite relatively high homology between the amino acid sequences of the bZIP motifs, these proteins recognize diverse DNA sequences. Here we report the 2.0 A resolution crystal structure of the bZIP motif of one such transcription factor, PAP1, a fission yeast AP-1-like transcription factor that binds DNA containing the novel consensus sequence TTACGTAA. The structure reveals how the Pap1-specific residues of the bZIP basic region recognize the target sequence and shows that the side chain of the invariant Asn in the bZIP motif adopts an alternative conformation in Pap1. This conformation, which is stabilized by a Pap1-specific residue and its associated water molecule, recognizes a different base in the target sequence from that in other bZIP subfamilies.

PubMed: 11017199
DOI: 10.1038/82822

Experimental method

X-RAY DIFFRACTION (2 Å)