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1tbx
From Proteopedia
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| - | [[Image:1tbx.jpg|left|200px]] | ||
| - | + | ==Crystal structure of SSV1 F-93== | |
| - | + | <StructureSection load='1tbx' size='340' side='right'caption='[[1tbx]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1tbx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_spindle-shaped_virus_1 Sulfolobus spindle-shaped virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TBX FirstGlance]. <br> | |
| - | | | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1tbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbx OCA], [https://pdbe.org/1tbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tbx RCSB], [https://www.ebi.ac.uk/pdbsum/1tbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tbx ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | ''' | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/F93_SSV1 F93_SSV1] Probable transcription factor that recognizes a (pseudo-)palindromic DNA target sequence. | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | == | + | == Publication Abstract from PubMed == |
Sulfolobus spindle-shaped viruses (SSVs), or Fuselloviridae, are ubiquitous crenarchaeal viruses found in high-temperature acidic hot springs around the world (pH </=4.0; temperature of >/=70 degrees C). Because they are relatively easy to isolate, they represent the best studied of the crenarchaeal viruses. This is particularly true for the type virus, SSV1, which contains a double-stranded DNA genome of 15.5 kilobases, encoding 34 putative open reading frames. Interestingly, the genome shows little sequence similarity to organisms other than its SSV homologues. Together, sequence similarity and biochemical analyses have suggested functions for only 6 of the 34 open reading frames. Thus, even though SSV1 is the best-studied crenarchaeal virus, functions for most (28) of its open reading frames remain unknown. We have undertaken biochemical and structural studies for the gene product of open reading frame F-93. We find that F-93 exists as a homodimer in solution and that a tight dimer is also present in the 2.7-A crystal structure. Further, the crystal structure reveals a fold that is homologous to the SlyA and MarR subfamilies of winged-helix DNA binding proteins. This strongly suggests that F-93 functions as a transcription factor that recognizes a (pseudo-)palindromic DNA target sequence. | Sulfolobus spindle-shaped viruses (SSVs), or Fuselloviridae, are ubiquitous crenarchaeal viruses found in high-temperature acidic hot springs around the world (pH </=4.0; temperature of >/=70 degrees C). Because they are relatively easy to isolate, they represent the best studied of the crenarchaeal viruses. This is particularly true for the type virus, SSV1, which contains a double-stranded DNA genome of 15.5 kilobases, encoding 34 putative open reading frames. Interestingly, the genome shows little sequence similarity to organisms other than its SSV homologues. Together, sequence similarity and biochemical analyses have suggested functions for only 6 of the 34 open reading frames. Thus, even though SSV1 is the best-studied crenarchaeal virus, functions for most (28) of its open reading frames remain unknown. We have undertaken biochemical and structural studies for the gene product of open reading frame F-93. We find that F-93 exists as a homodimer in solution and that a tight dimer is also present in the 2.7-A crystal structure. Further, the crystal structure reveals a fold that is homologous to the SlyA and MarR subfamilies of winged-helix DNA binding proteins. This strongly suggests that F-93 functions as a transcription factor that recognizes a (pseudo-)palindromic DNA target sequence. | ||
| - | + | Crystal structure of F-93 from Sulfolobus spindle-shaped virus 1, a winged-helix DNA binding protein.,Kraft P, Oeckinghaus A, Kummel D, Gauss GH, Gilmore J, Wiedenheft B, Young M, Lawrence CM J Virol. 2004 Nov;78(21):11544-50. PMID:15479795<ref>PMID:15479795</ref> | |
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| - | Crystal structure of F-93 from Sulfolobus spindle-shaped virus 1, a winged-helix DNA binding protein., Kraft P, Oeckinghaus A, Kummel D, Gauss GH, Gilmore J, Wiedenheft B, Young M, Lawrence CM | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1tbx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sulfolobus spindle-shaped virus 1]] | ||
| + | [[Category: Gauss GH]] | ||
| + | [[Category: Kraft P]] | ||
| + | [[Category: Kummel D]] | ||
| + | [[Category: Lawrence CM]] | ||
| + | [[Category: Oeckinghaus A]] | ||
| + | [[Category: Wiedenheft B]] | ||
| + | [[Category: Young M]] | ||
Current revision
Crystal structure of SSV1 F-93
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