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| | ==NON-SPECIFIC PROTEIN-DNA INTERACTIONS IN THE SSO7D-DNA COMPLEX, NMR, 1 STRUCTURE== | | ==NON-SPECIFIC PROTEIN-DNA INTERACTIONS IN THE SSO7D-DNA COMPLEX, NMR, 1 STRUCTURE== |
| - | <StructureSection load='1bbx' size='340' side='right'caption='[[1bbx]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1bbx' size='340' side='right'caption='[[1bbx]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bbx]] is a 4 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BBX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bbx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BBX FirstGlance]. <br> |
| - | </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=1bbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbx OCA], [http://pdbe.org/1bbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bbx RCSB], [http://www.ebi.ac.uk/pdbsum/1bbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbx ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1bbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbx OCA], [https://pdbe.org/1bbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bbx RCSB], [https://www.ebi.ac.uk/pdbsum/1bbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DN72_SULSO DN72_SULSO]] Constrain negative DNA supercoils; may be involved in maintaining the integrity of their genome at high temperature. Stimulates the Holliday junction cleavage activity of Hjc.<ref>PMID:11709558</ref> | + | [https://www.uniprot.org/uniprot/DN7D_SACS2 DN7D_SACS2] Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature (By similarity). Stimulates the Holliday junction cleavage activity of Hjc (PubMed:11709558).[UniProtKB:P61990]<ref>PMID:11709558</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Agback, P]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Baumann, H]] | + | [[Category: Agback P]] |
| - | [[Category: Hard, T]] | + | [[Category: Baumann H]] |
| - | [[Category: Knapp, S]] | + | [[Category: Hard T]] |
| - | [[Category: Ladenstein, R]] | + | [[Category: Knapp S]] |
| - | [[Category: Dna binding protein-dna complex]]
| + | [[Category: Ladenstein R]] |
| - | [[Category: Nonspecific protein-dna interaction]]
| + | |
| - | [[Category: Protein-dna interaction]]
| + | |
| Structural highlights
Function
DN7D_SACS2 Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature (By similarity). Stimulates the Holliday junction cleavage activity of Hjc (PubMed:11709558).[UniProtKB:P61990][1]
Publication Abstract from PubMed
Many biochemical processes, including DNA packing, maintenance and control, rely on non-sequence specific protein-DNA interactions. Nonspecific DNA-binding proteins have evolved to tolerate a wide range of DNA sequences, yet bind with a respectable affinity. The nonspecific binding requirement is in contrast to that imposed on, for example, transcription factors and implies a different structural basis for the biomolecular recognition process. To address this issue, and the mechanism for archaeal DNA packing, we determined the structure of the Sso7d protein from Sulfolobus solfataricus in complex with DNA. Sso7d binds DNA by placing a triple-stranded beta-sheet across the DNA minor groove. The protein is anchored in this position by the insertion of hydrogen bond-donating side chains into the groove and additionally stabilized by electrostatic and non-polar interactions with the DNA backbone. This structure explains how strong binding can be achieved independent of DNA sequence. Sso7d binding also distorts the DNA conformation and introduces significant unwinding of the helix. This effect suggests a mechanism for DNA packing in Sulfolobus based on negative DNA supercoiling.
Architecture of nonspecific protein-DNA interactions in the Sso7d-DNA complex.,Agback P, Baumann H, Knapp S, Ladenstein R, Hard T Nat Struct Biol. 1998 Jul;5(7):579-84. PMID:9665172[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kvaratskhelia M, Wardleworth BN, Bond CS, Fogg JM, Lilley DM, White MF. Holliday junction resolution is modulated by archaeal chromatin components in vitro. J Biol Chem. 2002 Jan 25;277(4):2992-6. Epub 2001 Nov 14. PMID:11709558 doi:http://dx.doi.org/10.1074/jbc.M109496200
- ↑ Agback P, Baumann H, Knapp S, Ladenstein R, Hard T. Architecture of nonspecific protein-DNA interactions in the Sso7d-DNA complex. Nat Struct Biol. 1998 Jul;5(7):579-84. PMID:9665172 doi:http://dx.doi.org/10.1038/836
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