1sap

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(New page: 200px<br /><applet load="1sap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sap" /> '''HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX ...)
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[[Image:1sap.gif|left|200px]]<br /><applet load="1sap" size="450" color="white" frame="true" align="right" spinBox="true"
 
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'''HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE'''<br />
 
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==Overview==
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==HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE==
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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.
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<StructureSection load='1sap' size='340' side='right'caption='[[1sap]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1SAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SAP OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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==Reference==
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</table>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7577913 7577913]
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== Function ==
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[[Category: Single protein]]
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[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]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sulfolobus acidocaldarius]]
[[Category: Sulfolobus acidocaldarius]]
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[[Category: Edmondson, S.P.]]
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[[Category: Edmondson SP]]
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[[Category: Shriver, J.W.]]
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[[Category: Shriver JW]]
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[[Category: dna-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:13:55 2007''
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HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE

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