1tvs
From Proteopedia
(New page: 200px<br /><applet load="1tvs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tvs" /> '''TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HEL...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1tvs.gif|left|200px]]<br /><applet load="1tvs" size=" | + | [[Image:1tvs.gif|left|200px]]<br /><applet load="1tvs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tvs" /> | caption="1tvs" /> | ||
'''TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN'''<br /> | '''TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of the 75-amino-acid trans-activator (Tat) protein | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TVS is a [http://en.wikipedia.org/wiki/Single_protein 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:// | + | 1TVS is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:51 2008'' |
Revision as of 13:17, 21 February 2008
|
TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN
Overview
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.
About this Structure
1TVS is a Single protein structure of sequence from Equine infectious anemia virus. Full crystallographic information is available from OCA.
Reference
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:7957222
Page seeded by OCA on Thu Feb 21 15:17:51 2008
