1jjh
From Proteopedia
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'''E2 DNA-binding Domain from Bovine Papillomavirus Type 1''' | '''E2 DNA-binding Domain from Bovine Papillomavirus Type 1''' | ||
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[[Category: Schapira, M.]] | [[Category: Schapira, M.]] | ||
[[Category: Wang, A F.]] | [[Category: Wang, A F.]] | ||
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| - | [[Category: | + | [[Category: E2]] |
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Revision as of 18:17, 2 May 2008
E2 DNA-binding Domain from Bovine Papillomavirus Type 1
Overview
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.
About this Structure
1JJH is a Single protein structure of sequence from Bovine papillomavirus type 1. Full crystallographic information is available from OCA.
Reference
Subunit rearrangement accompanies sequence-specific DNA binding by the bovine papillomavirus-1 E2 protein., Hegde RS, Wang AF, Kim SS, Schapira M, J Mol Biol. 1998 Mar 6;276(4):797-808. PMID:9500927 Page seeded by OCA on Fri May 2 21:17:57 2008
