1tvs
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1tvs.gif|left|200px]] | [[Image:1tvs.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1tvs", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1tvs| PDB=1tvs | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN''' | '''TRIFLUOROETHANOL STABILIZES A HELIX-TURN-HELIX MOTIF IN EQUINE INFECTIOUS-ANEMIA-VIRUS TRANS-ACTIVATOR PROTEIN''' | ||
| Line 27: | Line 24: | ||
[[Category: Roesch, P.]] | [[Category: Roesch, P.]] | ||
[[Category: Sticht, H.]] | [[Category: Sticht, H.]] | ||
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:25:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:25, 3 May 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 Sat May 3 10:25:54 2008
