Crystal structure of pu.1 ets domain-dna complex: a new pattern for helix-turn-helix recognition

F. Pio, R. Kodandapani, C. Z. Ni, G. Piccialli, S. McKercher, Michael Klemsz, R. A. Maki, K. R. Ely

Research output: Contribution to journalArticle

Abstract

The ets family of transcription factors regulate gene expression during growth and development and share a conserved ETS DNA-binding domain that binds as a monomer to the sequence 5′-C/AGGAA/T-3′. The crystal structure of the PU.1 ETS domain complexed with DNA has been determined at 2.3-Å resolution. The domain is similar to α+β ("winged") helix-turn-helix DNA-binding proteins and contacts a ten bp region of duplex DNA that is bent (8°) but uniformly curved without distinct kinks. Four conserved amino acids contact DNA from a novel loop-helix-loop architecture. Arg232 and Arg235 from the recognition helix are hydrogen-bonded to the GGA bases in the major groove. These interactions represent the paradigm for ets recognition. Two loops contact the DNA backbone in the minor groove: Lys245 in the "wing" between the third and fourth β-strands contacts the phosphate backbone of the GGAA strand upstream from the core sequence while Lys219 from the "turn" of the HTH motif contacts the phosphate backbone of the opposite strand downstream of the GGAA core. This work was supported by grants USAMRDC-DAMD17-94J-4439, NIH-CA63489-01 and NIH AI20194.

Original languageEnglish (US)
JournalFASEB Journal
Volume10
Issue number6
StatePublished - 1996
Externally publishedYes

Fingerprint

crystal structure
Crystal structure
DNA
phosphates
Helix-Turn-Helix Motifs
Proto-Oncogene Proteins c-ets
Phosphates
DNA-binding proteins
DNA-binding domains
Organized Financing
hydrogen
DNA-Binding Proteins
growth and development
Growth and Development
transcription factors
Gene expression
Hydrogen
Transcription Factors
gene expression
Monomers

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Pio, F., Kodandapani, R., Ni, C. Z., Piccialli, G., McKercher, S., Klemsz, M., ... Ely, K. R. (1996). Crystal structure of pu.1 ets domain-dna complex: a new pattern for helix-turn-helix recognition. FASEB Journal, 10(6).

Crystal structure of pu.1 ets domain-dna complex : a new pattern for helix-turn-helix recognition. / Pio, F.; Kodandapani, R.; Ni, C. Z.; Piccialli, G.; McKercher, S.; Klemsz, Michael; Maki, R. A.; Ely, K. R.

In: FASEB Journal, Vol. 10, No. 6, 1996.

Research output: Contribution to journalArticle

Pio, F, Kodandapani, R, Ni, CZ, Piccialli, G, McKercher, S, Klemsz, M, Maki, RA & Ely, KR 1996, 'Crystal structure of pu.1 ets domain-dna complex: a new pattern for helix-turn-helix recognition', FASEB Journal, vol. 10, no. 6.
Pio, F. ; Kodandapani, R. ; Ni, C. Z. ; Piccialli, G. ; McKercher, S. ; Klemsz, Michael ; Maki, R. A. ; Ely, K. R. / Crystal structure of pu.1 ets domain-dna complex : a new pattern for helix-turn-helix recognition. In: FASEB Journal. 1996 ; Vol. 10, No. 6.
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