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| | ==HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE== | | ==HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE== |
| - | <StructureSection load='1sap' size='340' side='right'caption='[[1sap]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1sap' size='340' side='right'caption='[[1sap]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sap]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SAP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sap]] 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=1SAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SAP FirstGlance]. <br> |
| - | </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=1sap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sap OCA], [https://pdbe.org/1sap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sap RCSB], [https://www.ebi.ac.uk/pdbsum/1sap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sap 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=1sap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sap OCA], [https://pdbe.org/1sap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sap RCSB], [https://www.ebi.ac.uk/pdbsum/1sap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sap ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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: Large Structures]] |
| - | [[Category: Edmondson, S P]] | + | [[Category: Sulfolobus acidocaldarius]] |
| - | [[Category: Shriver, J W]] | + | [[Category: Edmondson SP]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Shriver JW]] |
| - | [[Category: Dna-binding protein]]
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| 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
The Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius are a heterogeneous mixture of small, thermostable, nonspecific DNA-binding proteins. One of these proteins, Sac7d, has been overexpressed in Escherichia coli to provide a homogeneous preparation for structure, stability, and function studies. We present here essentially complete sequence-specific 1H NMR assignments for Sac7d, a delineation of secondary structural elements, and the high-resolution solution structure obtained from a full relaxation matrix refinement. The final structure provides an excellent fit to the NMR data with an NOE R-factor of 0.27 for backbone NOEs. The structure has a compact globular fold with 82% of the sequence involved in regular secondary structure: an antiparallel two-stranded beta-ribbon with a tight turn, followed by a short 3(10) helix, an antiparallel three-stranded beta-sheet, another short 3(10) helix, and finally four turns of alpha-helix. The amphipathic alpha-helix packs across the hydrophobic face of the three-stranded beta-sheet in an open-faced sandwich arrangement with at least one turn of the helix exposed beyond the sheet. The hydrophobic face of the beta-ribbon packs against a corner of the twisted beta-sheet. The single tryptophan responsible for the 88% fluorescence quenching upon DNA binding is exposed on the surface of the three-stranded beta-sheet. Lysines 5 and 7, whose monomethylation may be associated with enhanced thermostability, are highly solvent exposed along the inner edge of the two-stranded ribbon. The structure of Sac7d differs in many respects from that reported for the homologous native Sso7d [Baumann et al. (1994) Nature Struct. Biol. 1, 808] with a backbone RMSD greater than 3.0 A, largely due to the packing and length of the C-terminal alpha-helix which may be important in Sac7d DNA binding.
Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius.,Edmondson SP, Qiu L, Shriver JW Biochemistry. 1995 Oct 17;34(41):13289-304. PMID:7577913[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Edmondson SP, Qiu L, Shriver JW. Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry. 1995 Oct 17;34(41):13289-304. PMID:7577913
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