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| | ==NMR Structure of Sso10a, a Hyperthermophile DNA-binding Protein with an Extended Anti-parallel Coiled Coil== | | ==NMR Structure of Sso10a, a Hyperthermophile DNA-binding Protein with an Extended Anti-parallel Coiled Coil== |
| - | <StructureSection load='1xsx' size='340' side='right'caption='[[1xsx]], [[NMR_Ensembles_of_Models | 11 NMR models]]' scene=''> | + | <StructureSection load='1xsx' size='340' side='right'caption='[[1xsx]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xsx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xsx]] is a 2 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=1XSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSX FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sso10a ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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=1xsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsx OCA], [https://pdbe.org/1xsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsx RCSB], [https://www.ebi.ac.uk/pdbsum/1xsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsx 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=1xsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsx OCA], [https://pdbe.org/1xsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsx RCSB], [https://www.ebi.ac.uk/pdbsum/1xsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5W1E8_SACSO Q5W1E8_SACSO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Clark, A T]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Edmondson, S P]] | + | [[Category: Clark AT]] |
| - | [[Category: Kahsai, M A]] | + | [[Category: Edmondson SP]] |
| - | [[Category: Shriver, J W]] | + | [[Category: Kahsai MA]] |
| - | [[Category: Vogler, B]] | + | [[Category: Shriver JW]] |
| - | [[Category: Anti-parallel coiled coil dimer]] | + | [[Category: Vogler B]] |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Hyperthermophile dna-binding protein]]
| + | |
| - | [[Category: Winged helix-turn-helix]]
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| Structural highlights
Function
Q5W1E8_SACSO
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
Sso10a is one of a number of DNA-binding proteins from the hyperthermophile Sulfolobus solfataricus that has been associated with DNA packaging and chromatin regulation. Sequence analysis indicates that it is a member of a conserved group of archaeal transcription regulators (COG3432). We have determined the solution structure of Sso10a and show that it is a homodimer of winged-helix DNA-binding domains. The dimer interface consists of an extended antiparallel coiled coil, with the globular DNA-binding domains positioned at opposite ends of a solvent-exposed coiled-coil rod. NMR structure refinement of the elongated structure benefited not only from the inclusion of residual dipolar couplings from partially aligned samples but also the influence of anisotropic rotational diffusion on heteronuclear relaxation. An analysis of backbone mobility using (15)N relaxation rates indicated that the overall tertiary and quaternary structure is largely inflexible on the nanosecond to picosecond time scale. Amide hydrogen exchange data demonstrated that the most stable region of the protein extends from the core of the winged helices into the coiled coil. The positions of the globular heads relative to the coiled coil in solution deviate only slightly from that observed in a crystal structure. The most significant difference between the solution and crystal structures occurs in the putative DNA-binding helix-turn-helix (HTH) motif. This is the region of lowest stability in solution and a point of protein-protein contact in the crystal. Alternative conformations of the HTH motif may permit adjustment of the structure for optimal DNA binding.
Solution structure, stability, and flexibility of Sso10a: a hyperthermophile coiled-coil DNA-binding protein.,Kahsai MA, Vogler B, Clark AT, Edmondson SP, Shriver JW Biochemistry. 2005 Mar 1;44(8):2822-32. PMID:15723526[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kahsai MA, Vogler B, Clark AT, Edmondson SP, Shriver JW. Solution structure, stability, and flexibility of Sso10a: a hyperthermophile coiled-coil DNA-binding protein. Biochemistry. 2005 Mar 1;44(8):2822-32. PMID:15723526 doi:10.1021/bi047669t
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