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| | <StructureSection load='1o7i' size='340' side='right'caption='[[1o7i]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='1o7i' size='340' side='right'caption='[[1o7i]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o7i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacs2 Sacs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O7I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o7i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7i OCA], [http://pdbe.org/1o7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7i RCSB], [http://www.ebi.ac.uk/pdbsum/1o7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7i ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1o7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7i OCA], [https://pdbe.org/1o7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7i RCSB], [https://www.ebi.ac.uk/pdbsum/1o7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SSB_SACS2 SSB_SACS2] Binds to ssDNA, binding approximately 5 nucleotides per monomer. Binding my be slightly cooperative. Inhibits the endonuclease activity of XPF.<ref>PMID:12675797</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sacs2]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Kerr, I D]] | + | [[Category: Kerr ID]] |
| - | [[Category: Naismith, J H]] | + | [[Category: Naismith JH]] |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Dna-binding protein]]
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| - | [[Category: Ob fold]]
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| - | [[Category: Single stranded dna]]
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| Structural highlights
Function
SSB_SACS2 Binds to ssDNA, binding approximately 5 nucleotides per monomer. Binding my be slightly cooperative. Inhibits the endonuclease activity of XPF.[1]
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
Information processing pathways such as DNA replication are conserved in eukaryotes and archaea and are significantly different from those found in bacteria. Single-stranded DNA-binding (SSB) proteins (or replication protein A, RPA, in eukaryotes) play a central role in many of these pathways. However, whilst euryarchaea have a eukaryotic-type RPA homologue, crenarchaeal SSB proteins appear much more similar to the bacterial proteins, with a single OB fold for DNA binding and a flexible C-terminal tail that is implicated in protein-protein interactions. We have determined the crystal structure of the SSB protein from the crenarchaeote Sulfolobus solfataricus to 1.26 A. The structure shows a striking and unexpected similarity to the DNA-binding domains of human RPA, providing confirmation of the close relationship between archaea and eukaryotes. The high resolution of the structure, together with thermodynamic and mutational studies of DNA binding, allow us to propose a molecular basis for DNA binding and define the features required for eukaryotic and archaeal OB folds.
Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein.,Kerr ID, Wadsworth RI, Cubeddu L, Blankenfeldt W, Naismith JH, White MF EMBO J. 2003 Jun 2;22(11):2561-70. PMID:12773373[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Roberts JA, Bell SD, White MF. An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA. Mol Microbiol. 2003 Apr;48(2):361-71. doi: 10.1046/j.1365-2958.2003.03444.x. PMID:12675797 doi:http://dx.doi.org/10.1046/j.1365-2958.2003.03444.x
- ↑ Kerr ID, Wadsworth RI, Cubeddu L, Blankenfeldt W, Naismith JH, White MF. Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein. EMBO J. 2003 Jun 2;22(11):2561-70. PMID:12773373 doi:10.1093/emboj/cdg272
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