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| | ==Single stranded DNA-binding protein(ICP8) from Herpes simplex virus-1== | | ==Single stranded DNA-binding protein(ICP8) from Herpes simplex virus-1== |
| - | <StructureSection load='1urj' size='340' side='right' caption='[[1urj]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='1urj' size='340' side='right'caption='[[1urj]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1urj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hhv-1 Hhv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1URJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1urj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1URJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=1urj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urj OCA], [http://pdbe.org/1urj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1urj RCSB], [http://www.ebi.ac.uk/pdbsum/1urj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1urj ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1urj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urj OCA], [https://pdbe.org/1urj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1urj RCSB], [https://www.ebi.ac.uk/pdbsum/1urj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1urj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNBI_HHV11 DNBI_HHV11]] Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein UL9. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands.<ref>PMID:15078942</ref> <ref>PMID:7961904</ref> | + | [https://www.uniprot.org/uniprot/DNBI_HHV11 DNBI_HHV11] Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein UL9. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands.<ref>PMID:15078942</ref> <ref>PMID:7961904</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Single-stranded DNA-binding protein|Single-stranded DNA-binding protein]] | + | *[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hhv-1]] | + | [[Category: Human alphaherpesvirus 1]] |
| - | [[Category: Mapelli, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Panjikar, S]] | + | [[Category: Mapelli M]] |
| - | [[Category: Tucker, P A]] | + | [[Category: Panjikar S]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Tucker PA]] |
| - | [[Category: Dna replication]]
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| - | [[Category: Dna-binding]]
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| - | [[Category: Dna-binding protein]]
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| - | [[Category: Hsv-1]]
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| - | [[Category: Icp8]]
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| - | [[Category: Nuclear protein]]
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| - | [[Category: Ssb]]
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| - | [[Category: Zinc-finger]]
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| Structural highlights
Function
DNBI_HHV11 Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein UL9. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands.[1] [2]
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
All organisms including animal viruses use specific proteins to bind single-stranded DNA rapidly in a non-sequence-specific, flexible, and cooperative manner during the DNA replication process. The crystal structure of a 60-residue C-terminal deletion construct of ICP8, the major single-stranded DNA-binding protein from herpes simplex virus-1, was determined at 3.0 A resolution. The structure reveals a novel fold, consisting of a large N-terminal domain (residues 9-1038) and a small C-terminal domain (residues 1049-1129). On the basis of the structure and the nearest neighbor interactions in the crystal, we have presented a model describing the site of single-stranded DNA binding and explaining the basis for cooperative binding. This model agrees with the beaded morphology observed in electron micrographs.
The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding.,Mapelli M, Panjikar S, Tucker PA J Biol Chem. 2005 Jan 28;280(4):2990-7. Epub 2004 Oct 26. PMID:15507432[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reuven NB, Antoku S, Weller SK. The UL12.5 gene product of herpes simplex virus type 1 exhibits nuclease and strand exchange activities but does not localize to the nucleus. J Virol. 2004 May;78(9):4599-608. PMID:15078942
- ↑ Boehmer PE, Craigie MC, Stow ND, Lehman IR. Association of origin binding protein and single strand DNA-binding protein, ICP8, during herpes simplex virus type 1 DNA replication in vivo. J Biol Chem. 1994 Nov 18;269(46):29329-34. PMID:7961904
- ↑ Mapelli M, Panjikar S, Tucker PA. The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding. J Biol Chem. 2005 Jan 28;280(4):2990-7. Epub 2004 Oct 26. PMID:15507432 doi:10.1074/jbc.M406780200
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