Download MendeleySubunit rearrangement accompanies sequence-specific DNA binding by the bovine papillomavirus-1 E2 protein.
Hegde, R.S., Wang, A.F., Kim, S.S., Schapira, M.(1998) J Mol Biol 276: 797-808
- PubMed: 9500927
- DOI: https://doi.org/10.1006/jmbi.1997.1587
- Primary Citation of Related Structures:
1JJH - PubMed Abstract:
The 2.5 A crystal structures of the DNA-binding domain of the E2 protein from bovine papillomavirus strain 1 and its complex with DNA are presented. E2 is a transcriptional regulatory protein that is also involved in viral DNA replication. It is the structural prototype for a novel class of DNA-binding proteins: dimeric beta-barrels with surface alpha-helices that serve as recognition helices. These helices contain the amino-acid residues involved in sequence-specifying interactions. The E2 proteins from different papillomavirus strains recognize and bind to the same consensus 12 base-pair DNA sequence. However, recent evidence from solution studies points to differences in the mechanisms by which E2 from the related viral strains bovine papillomavirus-1 and human papillomavirus-16 discriminate between DNA targets based on non-contacted nucleotide sequences. This report provides evidence that sequence-specific DNA-binding is accompanied by a rearrangement of protein subunits and deformation of the DNA. These results suggest that, along with DNA sequence-dependent conformational properties, protein subunit orientation plays a significant role in the mechanisms of target selection utilized by E2.
Organizational Affiliation:
Department of Biochemistry and Program in Structural Biology, Skirball Institute of Biomolecular Medicine, New York University Medical Center, 540 First Avenue, New York, NY 10016, USA.
