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| | <StructureSection load='1jjh' size='340' side='right'caption='[[1jjh]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1jjh' size='340' side='right'caption='[[1jjh]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jjh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JJH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jjh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JJH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1by9|1by9]], [[2bop|2bop]], [[1f9f|1f9f]], [[1jj4|1jj4]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1by9|1by9]], [[2bop|2bop]], [[1f9f|1f9f]], [[1jj4|1jj4]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjh OCA], [http://pdbe.org/1jjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jjh RCSB], [http://www.ebi.ac.uk/pdbsum/1jjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjh ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjh OCA], [https://pdbe.org/1jjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jjh RCSB], [https://www.ebi.ac.uk/pdbsum/1jjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VE2_BPV1 VE2_BPV1]] E2 regulates viral transcription and DNA replication. Binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. Can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication. | + | [[https://www.uniprot.org/uniprot/VE2_BPV1 VE2_BPV1]] E2 regulates viral transcription and DNA replication. Binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. Can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1jjh" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1jjh" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Regulatory protein E2|Regulatory protein E2]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[VE2_BPV1] E2 regulates viral transcription and DNA replication. Binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. Can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hegde RS, Wang AF, Kim SS, Schapira M. Subunit rearrangement accompanies sequence-specific DNA binding by the bovine papillomavirus-1 E2 protein. J Mol Biol. 1998 Mar 6;276(4):797-808. PMID:9500927 doi:10.1006/jmbi.1997.1587
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