Subunit rearrangement accompanies sequence-specific DNA binding by the bovine papillomavirus-1 E2 protein

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• 作者：Hegde ; Rashmi S. ; Wang ; Ai-Fei ; Kim ; Seung-Sup ; Schapira ; Matthieu
• 关键词：papillomavirus ; protein-DNA ; crystal structure ; DNA-deformation ; E2 ; BPV ; bovine papillomavirus ; HPV ; human papillomavirus
• 刊名：Journal of Molecular Biology
• 出版年：1998
• 出版时间：March 6, 1998
• 年：1998
• 卷：276
• 期：4
• 页码：797-808
• 全文大小：1.50 M

文摘

The 2.5 Å 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 β-barrels with surface α-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.