1PUE

PU.1 ETS DOMAIN-DNA COMPLEX

Summary for 1PUE

• Entry DOI: 10.2210/pdb1pue/pdb
• Descriptor: DNA (5'-D(*AP*AP*AP*AP*AP*GP*GP*GP*GP*AP*AP*GP*TP*GP*GP*G)-3'), DNA (5'-D(*TP*CP*CP*CP*AP*CP*TP*TP*CP*CP*CP*CP*TP*TP*TP*T)-3'), PROTEIN (TRANSCRIPTION FACTOR PU.1 (TF PU.1)), ... (4 entities in total)
• Functional Keywords: complex (transcription regulating-dna), oncogene, transforming protein, dna- binding, activator, nuclear protein, transcription-dna complex, transcription/dna
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus: P17433
• Total number of polymer chains: 6
• Total formula weight: 40809.70

Authors

Kodandapani, R.,Pio, F.,Ni, C.Z.,Piccialli, G.,Klemsz, M.,McKercher, S.,Maki, R.A.,Ely, K.R. (deposition date: 1996-07-08, release date: 1997-02-12, Last modification date: 2024-02-14)

Primary citation

Kodandapani, R.,Pio, F.,Ni, C.Z.,Piccialli, G.,Klemsz, M.,McKercher, S.,Maki, R.A.,Ely, K.R.
A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex.
Nature, 380:456-460, 1996

PubMed Abstract: The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand.

PubMed: 8602247
DOI: 10.1038/380456a0

Experimental method

X-RAY DIFFRACTION (2.1 Å)