1b4b: Difference between revisions

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~~'''~~STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS~~'''~~

===STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS===

~~==Overview==~~

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The ~~arginine repressor (ArgR) is a hexameric DNA-binding protein that plays a multifunctional role in the bacterial cell. Here~~, ~~we present~~ the ~~2.5 A structure of apo-ArgR from Bacillus stearothermophilus and~~ the 2.~~2 A structure of the hexameric ArgR oligomerization domain with bound arginine~~. ~~This first view of intact ArgR reveals an approximately 32-symmetric hexamer of identical subunits~~, ~~with six DNA-binding domains surrounding a central oligomeric core~~. ~~The difference in quaternary organization of subunits in the arginine~~-~~bound and apo forms provides a possible explanation for poor operator binding by apo~~-~~ArgR and for high affinity binding in the presence of arginine.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10331868}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10331868 is the PubMed ID number.

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==About this Structure==

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[[Category: Oligomerization domain]]

[[Category: Repressor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:02:58 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:13:09 2008''

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-[[Image:1b4b.jpg|left|200px]]
+{{Seed}}
+[[Image:1b4b.png|left|200px]]
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 {{STRUCTURE_1b4b|  PDB=1b4b  |  SCENE=  }}
-'''STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS'''
+===STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS===
-==Overview==
+<!--
-The arginine repressor (ArgR) is a hexameric DNA-binding protein that plays a multifunctional role in the bacterial cell. Here, we present the 2.5 A structure of apo-ArgR from Bacillus stearothermophilus and the 2.2 A structure of the hexameric ArgR oligomerization domain with bound arginine. This first view of intact ArgR reveals an approximately 32-symmetric hexamer of identical subunits, with six DNA-binding domains surrounding a central oligomeric core. The difference in quaternary organization of subunits in the arginine-bound and apo forms provides a possible explanation for poor operator binding by apo-ArgR and for high affinity binding in the presence of arginine.
+The line below this paragraph, {{ABSTRACT_PUBMED_10331868}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10331868 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10331868}}
 ==About this Structure==
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 [[Category: Oligomerization domain]]
 [[Category: Repressor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:02:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:13:09 2008''