1mp9: Difference between revisions

Line 1:

[[Image:1mp9.~~gif~~|left|200px]]

[[Image:1mp9.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius~~'''~~

===TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius===

~~==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 line below this paragraph, {{ABSTRACT_PUBMED_14725775}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14725775 is the PubMed ID number.

-->

==About this Structure==

Line 31:

Line 35:

[[Category: Transcription factor]]

[[Category: Transcription regulation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ 3 01:33:06 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:40:12 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1mp9.gif|left|200px]]
+{{Seed}}
+[[Image:1mp9.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1mp9|  PDB=1mp9  |  SCENE=  }}
-'''TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius'''
+===TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_14725775}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14725775 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14725775}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Transcription factor]]
 [[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:33:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 00:40:12 2008''