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| | ==NMR structure of plasmid copy control protein ORF56 from sulfolobus islandicus== | | ==NMR structure of plasmid copy control protein ORF56 from sulfolobus islandicus== |
| - | <StructureSection load='2k9i' size='340' side='right'caption='[[2k9i]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k9i' size='340' side='right'caption='[[2k9i]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k9i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"sulfolobus_islandicus"_zillig_et_al._1994 "sulfolobus islandicus" zillig et al. 1994]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2K9I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k9i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus Sulfolobus islandicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K9I FirstGlance]. <br> |
| - | </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=2k9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9i OCA], [http://pdbe.org/2k9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k9i RCSB], [http://www.ebi.ac.uk/pdbsum/2k9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9i 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=2k9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9i OCA], [https://pdbe.org/2k9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k9i RCSB], [https://www.ebi.ac.uk/pdbsum/2k9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q54323_SULIS Q54323_SULIS] |
| - | ORF56 is a small and thermodynamically extremely stable dimeric protein from the archaeon Sulfolobus islandicus. This DNA binding protein is encoded on plasmid pRN1 and possibly controls the copy number of the plasmid. We report the solution NMR structure as well as the crystal structure of ORF56 comprising a ribbon-helix-helix fold. The homodimer consists of an antiparallel intersubunit beta-sheet and two alpha-helices per monomer, which is a common DNA binding fold of plasmid- and phage-encoded gene regulation proteins. NMR titration experiments with ORF56 and double-stranded DNA derived from its promoter binding site revealed that it is largely the beta-sheets that interact with the DNA. The beta-sheet experiences high local fluctuations, which are conserved among DNA binding ribbon-helix-helix dimers from mesophilic and hyperthermophilic organisms. In contrast, residues strongly protected against H-D exchange are localized in helix 2, forming the hydrophobic intermolecular core of the dimer. A structure-based comparison of the intermolecular binding surface and the change in accessible surface area upon unfolding of various ribbon-helix-helix dimers with the Gibbs free energy changes and m values show a correlation between hydrophobicity of these surface areas and stability. These findings provide possible explanations for the very high thermodynamic stability of ORF56 with retained DNA binding capacity.
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| - | Structure-Based Stability Analysis of an Extremely Stable Dimeric DNA Binding Protein from Sulfolobus islandicus.,Weininger U, Zeeb M, Neumann P, Low C, Stubbs MT, Lipps G, Balbach J Biochemistry. 2009 Oct 27;48(42):10030-7. PMID:19788170<ref>PMID:19788170</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 2k9i" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Sulfolobus islandicus zillig et al. 1994]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Balbach, J]] | + | [[Category: Sulfolobus islandicus]] |
| - | [[Category: Weininger, U]] | + | [[Category: Balbach J]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Weininger U]] |
| - | [[Category: Plasmid copy control protein]]
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| - | [[Category: Ribbon helix helix protein]]
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