Nuclear magnetic resonance-based model of a TF1/HmU-DNA complex

Archives of Biochemistry and Biophysics
M V SilvaD R Kearns

Abstract

Transcription factor 1 (TF1), a type II DNA-binding protein encoded by the Bacillus subtilis bacteriophage SPO1, has the capacity for sequence-selective DNA binding and a preference for 5-hydroxymethyl-2'-deoxyuridine (HmU)-containing DNA. In NMR studies of the TF1/HmU-DNA complex, intermolecular NOEs indicate that the flexible beta-ribbon and C-terminal alpha-helix are involved in the DNA-binding site of TF1, placing it in the beta-sheet category of DNA-binding proteins proposed to bind by wrapping two beta-ribbon "arms" around the DNA. Intermolecular and intramolecular NOEs were used to generate an energy-minimized model of the protein-DNA complex in which both DNA bending and protein structure changes are evident.

References

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Citations

Oct 16, 1999·Nucleic Acids Research·H M VuD R Kearns
Nov 11, 2006·IDrugs : the Investigational Drugs Journal·Letitia Perry, Andrew Balfe

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