1mp9: Difference between revisions

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[[Image:1mp9.gif|left|200px]]<br /><applet load="1mp9" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1mp9.gif|left|200px]]<br /><applet load="1mp9" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1mp9, resolution 2.000Å" />

'''TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius'''<br />

==Overview==

The crystal structure of TATA binding protein (TBP) from a, mesothermophilic archaeon, Sulfolobus acidocaldarius, has been determined, at a resolution of 2.0 A with an R factor of 20.9%. By comparing this, structure with the structures of TBPs from a hyperthermophilic archaeon, and mesophilic eukaryotes, as well as by comparing amino acid sequences of, TBPs from archaea, covering a wide range of optimum growth temperatures, two significant determinants of the stability of TBP have been identified:, increasing the interior hydrophobicity by interaction between three, residues, Val, Leu, and Ile, with further differentiation of the surface, and increasing its hydrophilicity and raising the cost of unfolding. These, findings suggest directions along which the stability of TBP can be, engineered.

The crystal structure of TATA binding protein (TBP) from a mesothermophilic archaeon, Sulfolobus acidocaldarius, has been determined at a resolution of 2.0 A with an R factor of 20.9%. By comparing this structure with the structures of TBPs from a hyperthermophilic archaeon and mesophilic eukaryotes, as well as by comparing amino acid sequences of TBPs from archaea, covering a wide range of optimum growth temperatures, two significant determinants of the stability of TBP have been identified: increasing the interior hydrophobicity by interaction between three residues, Val, Leu, and Ile, with further differentiation of the surface, and increasing its hydrophilicity and raising the cost of unfolding. These findings suggest directions along which the stability of TBP can be engineered.

==About this Structure==

1MP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1MP9 OCA].

1MP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP9 OCA].

==Reference==

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[[Category: transcription regulation]]

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@@ Line 1: / Line 1: @@
-[[Image:1mp9.gif|left|200px]]<br /><applet load="1mp9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mp9.gif|left|200px]]<br /><applet load="1mp9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mp9, resolution 2.000&Aring;" />
 '''TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius'''<br />
 ==Overview==
-The crystal structure of TATA binding protein (TBP) from a, mesothermophilic archaeon, Sulfolobus acidocaldarius, has been determined, at a resolution of 2.0 A with an R factor of 20.9%. By comparing this, structure with the structures of TBPs from a hyperthermophilic archaeon, and mesophilic eukaryotes, as well as by comparing amino acid sequences of, TBPs from archaea, covering a wide range of optimum growth temperatures, two significant determinants of the stability of TBP have been identified:, increasing the interior hydrophobicity by interaction between three, residues, Val, Leu, and Ile, with further differentiation of the surface, and increasing its hydrophilicity and raising the cost of unfolding. These, findings suggest directions along which the stability of TBP can be, engineered.
+The crystal structure of TATA binding protein (TBP) from a mesothermophilic archaeon, Sulfolobus acidocaldarius, has been determined at a resolution of 2.0 A with an R factor of 20.9%. By comparing this structure with the structures of TBPs from a hyperthermophilic archaeon and mesophilic eukaryotes, as well as by comparing amino acid sequences of TBPs from archaea, covering a wide range of optimum growth temperatures, two significant determinants of the stability of TBP have been identified: increasing the interior hydrophobicity by interaction between three residues, Val, Leu, and Ile, with further differentiation of the surface, and increasing its hydrophilicity and raising the cost of unfolding. These findings suggest directions along which the stability of TBP can be engineered.
 ==About this Structure==
-MP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MP9 OCA].
+MP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP9 OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:36:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:39 2008''