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

JOURNAL OF MOLECULAR BIOLOGY

卷:276

Article

Hegde, RS ; Wang, AF ; Kim, SS ; Schapira, M

关键词: papillomavirus;    protein-DNA;    crystal structure;    DNA-deformation;    E2;   

DOI  :  10.1006/jmbi.1997.1587

来源: Elsevier

【 摘 要 】

The 2.5 Angstrom 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. (C) 1998 Academic Press Limited.

【 授权许可】

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