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| | ==NMR Structure of the W24A Mutant of the Hyperthermophile Sac7d Protein== | | ==NMR Structure of the W24A Mutant of the Hyperthermophile Sac7d Protein== |
| - | <StructureSection load='1xx8' size='340' side='right' caption='[[1xx8]], [[NMR_Ensembles_of_Models | 11 NMR models]]' scene=''> | + | <StructureSection load='1xx8' size='340' side='right'caption='[[1xx8]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xx8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xx8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XX8 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sap|1sap]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sac7d ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909])</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=1xx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xx8 OCA], [https://pdbe.org/1xx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xx8 RCSB], [https://www.ebi.ac.uk/pdbsum/1xx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xx8 ProSAT]</span></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=1xx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xx8 OCA], [http://pdbe.org/1xx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xx8 RCSB], [http://www.ebi.ac.uk/pdbsum/1xx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xx8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DN71_SULAC DN71_SULAC]] Constrain negative DNA supercoils; may be involved in maintaining the integrity of their genome at high temperature. | + | [https://www.uniprot.org/uniprot/DN7D_SULAC DN7D_SULAC] Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.[UniProtKB:P61990] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33909]] | + | [[Category: Large Structures]] |
| - | [[Category: Bedell, J L]] | + | [[Category: Sulfolobus acidocaldarius]] |
| - | [[Category: Edmondson, S P]] | + | [[Category: Bedell JL]] |
| - | [[Category: Shriver, J W]] | + | [[Category: Edmondson SP]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Shriver JW]] |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Hyperthermophile]]
| + | |
| Structural highlights
Function
DN7D_SULAC Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.[UniProtKB:P61990]
Publication Abstract from PubMed
Sac7d is a small, chromatin protein from Sulfolobus acidocaldarius which induces a sharp kink in DNA with intercalation of valine and methionine side chains. The crystal structure of the protein-DNA complex indicates that a surface tryptophan (W24) plays a key role in DNA binding by hydrogen bonding to the DNA at the kink site. We show here that substitution of the solvent-exposed tryptophan with alanine (W24A) led to a significant loss in not only DNA binding affinity but also protein stability. The W24A substitution proved to be one of the most destabilizing surface substitutions in Sac7d. A global linkage analysis of the pH and salt dependence of stability indicated that the protein stability surface (DeltaG vs temperature, pH, and salt concentration) was lowered overall by 2 kcal/mol (from 0 to 100 degrees C, pH 0 to 7, and 0 to 0.3 M KCl). The lower free energy of unfolding could not be attributed to significant structural perturbations of surface electrostatic interactions. Residual dipolar coupling of partially aligned protein and the NMR solution structure of W24A confirmed that the surface substitution resulted in no significant change in structure. Stabilization of this hyperthermophile protein and its DNA complex by a surface cluster of hydrophobic residues involving W24 and the two intercalating side chains is discussed.
Role of a surface tryptophan in defining the structure, stability, and DNA binding of the hyperthermophile protein Sac7d.,Bedell JL, Edmondson SP, Shriver JW Biochemistry. 2005 Jan 25;44(3):915-25. PMID:15654747[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bedell JL, Edmondson SP, Shriver JW. Role of a surface tryptophan in defining the structure, stability, and DNA binding of the hyperthermophile protein Sac7d. Biochemistry. 2005 Jan 25;44(3):915-25. PMID:15654747 doi:10.1021/bi047823b
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