1jjh

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(New page: 200px<br /><applet load="1jjh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjh, resolution 2.50&Aring;" /> '''E2 DNA-binding Domai...)
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[[Image:1jjh.gif|left|200px]]<br /><applet load="1jjh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jjh, resolution 2.50&Aring;" />
caption="1jjh, resolution 2.50&Aring;" />
'''E2 DNA-binding Domain from Bovine Papillomavirus Type 1'''<br />
'''E2 DNA-binding Domain from Bovine Papillomavirus Type 1'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1JJH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JJH OCA].
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1JJH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJH OCA].
==Reference==
==Reference==
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[[Category: Bovine papillomavirus type 1]]
[[Category: Bovine papillomavirus type 1]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hegde, R.S.]]
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[[Category: Hegde, R S.]]
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[[Category: Kim, S.S.]]
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[[Category: Kim, S S.]]
[[Category: Schapira, M.]]
[[Category: Schapira, M.]]
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[[Category: Wang, A.F.]]
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[[Category: Wang, A F.]]
[[Category: bpv-1]]
[[Category: bpv-1]]
[[Category: dna-binding domain]]
[[Category: dna-binding domain]]
[[Category: e2]]
[[Category: e2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:19:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:24 2008''

Revision as of 11:23, 21 February 2008


1jjh, resolution 2.50Å

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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

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