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| - | ==STRUCTURE OF A DNA BINDING WINGED-HELIX PROTEIN, F-112, FROM SULFOLOBUS SPINDLE-SHAPED VIRUS 1.== | + | ==Structure of a DNA binding winged-helix protein, F-112, from Sulfolobus Spindle-shaped Virus 1.== |
| - | <StructureSection load='2vqc' size='340' side='right' caption='[[2vqc]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2vqc' size='340' side='right'caption='[[2vqc]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ssv1 Ssv1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cmx 2cmx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VQC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_spindle-shaped_virus_1 Sulfolobus spindle-shaped virus 1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cmx 2cmx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQC FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqc OCA], [http://pdbe.org/2vqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vqc RCSB], [http://www.ebi.ac.uk/pdbsum/2vqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vqc 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=2vqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqc OCA], [https://pdbe.org/2vqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vqc RCSB], [https://www.ebi.ac.uk/pdbsum/2vqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vqc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F112_SSV1 F112_SSV1] Essential for virus function.<ref>PMID:10430570</ref> |
| | <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: Ssv1]] | + | [[Category: Large Structures]] |
| - | [[Category: Corn, G J]] | + | [[Category: Sulfolobus spindle-shaped virus 1]] |
| - | [[Category: Kraft, P]] | + | [[Category: Corn GJ]] |
| - | [[Category: Lawrence, C M]] | + | [[Category: Kraft P]] |
| - | [[Category: Menon, S K]] | + | [[Category: Lawrence CM]] |
| - | [[Category: Wiedenheft, B]] | + | [[Category: Menon SK]] |
| - | [[Category: Young, M J]] | + | [[Category: Wiedenheft B]] |
| - | [[Category: Crenarchaeal]]
| + | [[Category: Young MJ]] |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Ssv]]
| + | |
| - | [[Category: Sulfolobus spindle virus]]
| + | |
| - | [[Category: Thermophilic protein]]
| + | |
| - | [[Category: Winged-helix]]
| + | |
| Structural highlights
Function
F112_SSV1 Essential for virus function.[1]
Publication Abstract from PubMed
Fuselloviridae are ubiquitous crenarchaeal viruses found in high-temperature acidic hot springs worldwide. The type virus, Sulfolobus spindle-shaped virus 1 (SSV1), has a double-stranded DNA genome that contains 34 open reading frames (ORFs). Fuselloviral genomes show little similarity to other organisms, generally precluding functional predictions. However, tertiary protein structure can provide insight into protein function. We have thus undertaken a systematic investigation of the SSV1 proteome and report here on the F112 gene product. Biochemical, proteomic and structural studies reveal a monomeric intracellular protein that adopts a winged helix DNA binding fold. Notably, the structure contains an intrachain disulfide bond, prompting analysis of cysteine usage in this and other hyperthermophilic viral genomes. The analysis supports a general abundance of disulfide bonds in the intracellular proteins of hyperthermophilic viruses, and reveals decreased cysteine content in the membrane proteins of hyperthermophilic viruses infecting Sulfolobales. The evolutionary implications of the SSV1 distribution are discussed.
Cysteine usage in Sulfolobus spindle-shaped virus 1 and extension to hyperthermophilic viruses in general.,Menon SK, Maaty WS, Corn GJ, Kwok SC, Eilers BJ, Kraft P, Gillitzer E, Young MJ, Bothner B, Lawrence CM Virology. 2008 Jul 5;376(2):270-8. Epub 2008 May 8. PMID:18471851[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stedman KM, Schleper C, Rumpf E, Zillig W. Genetic requirements for the function of the archaeal virus SSV1 in Sulfolobus solfataricus: construction and testing of viral shuttle vectors. Genetics. 1999 Aug;152(4):1397-405. PMID:10430570
- ↑ Menon SK, Maaty WS, Corn GJ, Kwok SC, Eilers BJ, Kraft P, Gillitzer E, Young MJ, Bothner B, Lawrence CM. Cysteine usage in Sulfolobus spindle-shaped virus 1 and extension to hyperthermophilic viruses in general. Virology. 2008 Jul 5;376(2):270-8. Epub 2008 May 8. PMID:18471851 doi:http://dx.doi.org/S0042-6822(08)00196-7
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