1FYL

SERENDIPITOUS CRYSTAL STRUCTURE CONTAINING THE HEAT SHOCK TRANSCRIPTION FACTOR'S DNA BINDING DOMAIN AND COGNATE DNA IN A HEAD-TO-HEAD ORIENTATION

Summary for 1FYL

• Entry DOI: 10.2210/pdb1fyl/pdb
• Related: 1FYK 1FYM 2HTS 3HTS
• Descriptor: HEAD-TO-HEAD HSE, HEAT SHOCK FACTOR PROTEIN (3 entities in total)
• Functional Keywords: crystal-packing interface, crystallization, protein-dna interface, protein-protein interface, static disorder, transcription-dna complex, transcription/dna
• Biological source: Kluyveromyces lactis; More
• Total number of polymer chains: 4
• Total formula weight: 29636.48

Authors

Littlefield, O.,Nelson, H.C.M. (deposition date: 2000-10-02, release date: 2001-09-28, Last modification date: 2024-10-30)

Primary citation

Littlefield, O.,Nelson, H.C.
Crystal packing interaction that blocks crystallization of a site-specific DNA binding protein-DNA complex.
Proteins, 45:219-228, 2001

PubMed Abstract: We present here three high-resolution crystal structures of complexes between the DNA-binding domain of the heat-shock transcription factor (HSF) and DNA oligomers. Although the DNA oligomers contain HSF's specific binding sequence, called a heat-shock element, the crystal structures do not contain the specific protein-DNA complex. In one crystal structure, the 10 base pair DNA oligomer is statically disordered. In the other two related structures, the 12 base pair DNA oligomers are in unique positions, but the protein-DNA contacts in these two crystals are not sequence specific. In all three structures, the DNA appears to act as a rigid, polyanion scaffold to support columns of proteins in a crystalline lattice. A robust crystal packing interface between protein monomers obscures the true DNA-binding surface, known from previous genetic and biochemical studies. By redesigning the protein to interfere with the crystal lattice contacts, we were able to obtain physiologically relevant crystals in a specific protein-DNA complex. Thus, a crystal-packing interface was able to prevent the weak, but physiological relevant interactions between a protein and DNA.

PubMed: 11599025
DOI: 10.1002/prot.1142

Experimental method

X-RAY DIFFRACTION (2.1 Å)