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1tvs

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[[Image:1tvs.gif|left|200px]]
 
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{{Structure
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==TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN==
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|PDB= 1tvs |SIZE=350|CAPTION= <scene name='initialview01'>1tvs</scene>
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<StructureSection load='1tvs' size='340' side='right'caption='[[1tvs]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1tvs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TVS FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE= POTENTIAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11665 Equine infectious anemia virus])
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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=1tvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tvs OCA], [https://pdbe.org/1tvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tvs RCSB], [https://www.ebi.ac.uk/pdbsum/1tvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tvs ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tvs OCA], [http://www.ebi.ac.uk/pdbsum/1tvs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tvs RCSB]</span>
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[https://www.uniprot.org/uniprot/O89467_9RETR O89467_9RETR]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tv/1tvs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tvs ConSurf].
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<div style="clear:both"></div>
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'''TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN'''
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==See Also==
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*[[Tat protein|Tat protein]]
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__TOC__
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==Overview==
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</StructureSection>
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The solution structure of the 75-amino-acid trans-activator (Tat) protein of the equine infectious-anemia virus in trifluoroethanol-containing solution was determined by two-dimensional and three-dimensional nuclear magnetic resonance spectroscopy, resulting in a total of 838 nuclear-Over-hauser-enhancement distance restraints, and restrained molecular-dynamics simulations. In contrast to the recently determined structure of this protein in trifluoroethanol-free pH 6.3 solution, the hydrophobic core and the adjacent basic RNA-binding region of the protein showed well-defined alpha-helical secondary structure in trifluoroethanol-containing solution. The helical regions comprise those parts of the molecule whose helix-forming tendencies were noted earlier in trifluoroethanol-free solution. Two helices (Gln38-Arg43 and Asp48-Ala64) are connected by a tight type-II turn centered at the strictly conserved Gly46 leading to a helix-turn-helix motif in the core and basic region of the protein. A third helix (Thr9-Asn13) is located in the less well defined N-terminal part of the protein. These observations may support the notion that the protein adopts a helical structure in the RNA-binding region on complex formation. Although the secondary-structure elements become better defined in trifluoroethanol-containing solution, the opposite is true for the hydrophobically stabilized tertiary structure. This adds a caveat to studies of protein structures in trifluoroethanol-containing solution in general.
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==About this Structure==
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1TVS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVS OCA].
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==Reference==
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Trifluoroethanol stabilizes a helix-turn-helix motif in equine infectious-anemia-virus trans-activator protein., Sticht H, Willbold D, Ejchart A, Rosin-Arbesfeld R, Yaniv A, Gazit A, Rosch P, Eur J Biochem. 1994 Nov 1;225(3):855-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7957222 7957222]
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[[Category: Equine infectious anemia virus]]
[[Category: Equine infectious anemia virus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Roesch, P.]]
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[[Category: Roesch P]]
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[[Category: Sticht, H.]]
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[[Category: Sticht H]]
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[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:53 2008''
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Current revision

TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN

PDB ID 1tvs

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