Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target.
The dominant transcriptional regulator of the papillomaviruses, E2, binds to its specific DNA target through a previously unobserved dimeric antiparallel beta-barrel. The DNA is severely but smoothly bent over the barrel by the interaction of successive major grooves with a pair of symmetrically disposed alpha-helices. The specific interface is an 'interwoven' network of interactions where the identifying base pairs of the target contact more than one amino-acid side chain and the discriminating amino acids interact with more than one base pair.
Hegde
R S
RS
Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510.
Grossman
S R
SR
Laimins
L A
LA
Sigler
P B
PB
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D052688:Bovine papillomavirus 1 / Q000235:genetics*; D003460:Crystallization; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D017510:Protein Folding; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
D004268:DNA-Binding Proteins; C051550:E2 protein, Bovine papillomavirus; D046911:Macromolecular Substances; D014764:Viral Proteins; D004247:DNA