Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DMA-binding domain bound to its DNA target

The dominant transcriptional regulator of the papiIlomaviruses, E2, binds to its specific DNA target through a previously unobserved dimeric ant i para I lei β-barrel. The DNA is severely but smoothly bent over the barrel by the interaction of successive major grooves with a pair of symmetrically disposed α-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.

[1]  S. Phillips.  Specific β-sheet interactions , 1991 .

[2]  D. Lowy,et al.  Bovine papillomavirus E2 trans-activating gene product binds to specific sites in papillomavirus DNA , 1987, Nature.

[3]  T. Blundell,et al.  Atomic Positions in Rhombohedral 2-Zinc Insulin Crystals , 1971, Nature.

[4]  M. Botchan,et al.  Activation of BPV-1 replication in vitro by the transcription factor E2 , 1991, Nature.

[5]  T. Steitz,et al.  Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees , 1991, Science.

[6]  Carl O. Pabo,et al.  Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: A framework for understanding homeodomain-DNA interactions , 1990, Cell.

[7]  K. Yamamoto,et al.  Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA , 2003, Nature.

[8]  E Westhof,et al.  Crystallographic refinement of yeast aspartic acid transfer RNA. , 1985, Journal of molecular biology.

[9]  G. Rose,et al.  Helix signals in proteins. , 1988, Science.

[10]  J. Richardson,et al.  Amino acid preferences for specific locations at the ends of alpha helices. , 1988, Science.

[11]  M. Botchan,et al.  The activation domain of the bovine papillomavirus E2 protein mediates association of DNA-bound dimers to form DNA loops. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[12]  E. Androphy,et al.  Cooperative binding of the E2 protein of bovine papillomavirus to adjacent E2-responsive sequences , 1991, Journal of virology.

[13]  Jordan,et al.  Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions , 1988, Science.

[14]  M Ptashne,et al.  Recognition of a DNA operator by the repressor of phage 434: a view at high resolution , 1988, Science.

[15]  A. Travers.  DNA bending and kinking — sequence dependence and function , 1991 .

[16]  Michael Carey,et al.  DNA recognition by GAL4: structure of a protein-DNA complex , 1992, Nature.

[17]  T. A. Jones,et al.  A graphics model building and refinement system for macromolecules , 1978 .

[18]  M. Botchan,et al.  Specific recognition nucleotides and their DNA context determine the affinity of E2 protein for 17 binding sites in the BPV-1 genome. , 1989, Genes & development.

[19]  R. Schlegel,et al.  The carboxy‐terminal domain shared by the bovine papillomavirus E2 transactivator and repressor proteins contains a specific DNA binding activity. , 1988, The EMBO journal.

[20]  M. Yaniv,et al.  Control of papillomavirus gene expression. , 1990, Biochimica et biophysica acta.

[21]  A. Joachimiak,et al.  Crystal structure of trp represser/operator complex at atomic resolution , 1988, Nature.

[22]  E. Androphy,et al.  Amino acids necessary for DNA contact and dimerization imply novel motifs in the papillomavirus E2 trans-activator. , 1992, Genes & development.

[23]  R. Kaptein,et al.  Structure of Arc represser in solution: evidence for a family of β-sheet DMA-binding proteins , 1990, Nature.

[24]  Jeffrey C. Hall.  Cycling transcripts and the circadian clock , 1991, Current Biology.

[25]  N. Seeman,et al.  Sequence-specific Recognition of Double Helical Nucleic Acids by Proteins (base Pairs/hydrogen Bonding/recognition Fidelity/ion Binding) , 2022 .

[26]  M. Yaniv,et al.  A dimer of BPV‐1 E2 containing a protease resistant core interacts with its DNA target. , 1988, The EMBO journal.

[27]  K. Watenpaugh,et al.  NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[28]  M. Yaniv,et al.  Structural and mutational analysis of E2 trans‐activating proteins of papillomaviruses reveals three distinct functional domains. , 1988, The EMBO journal.

[29]  R Lavery,et al.  The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids. , 1988, Journal of biomolecular structure & dynamics.

[30]  B. Finzel.  Incorporation of fast Fourier transforms to speed restrained least‐squares refinement of protein structures , 1987 .

[31]  L. Villarreal.  Common mechanisms of transformation by small DNA tumor viruses , 1989 .

[32]  P. Kraulis.  A program to produce both detailed and schematic plots of protein structures , 1991 .

[33]  B. Matthews,et al.  The molecular basis of DNA–protein recognition inferred from the structure of cro repressor , 1982, Nature.

[34]  J. Gauthier,et al.  The papillomavirus E2 protein: a factor with many talents. , 1991, Trends in biochemical sciences.

[35]  C. Moskaluk,et al.  DNA bending is induced in an enhancer by the DNA-binding domain of the bovine papillomavirus E2 protein. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[36]  P. Howley,et al.  E2 polypeptides encoded by bovine papillomavirus type 1 form dimers through the common carboxyl-terminal domain: transactivation is mediated by the conserved amino-terminal domain. , 1989, Proceedings of the National Academy of Sciences of the United States of America.