1o7x: Difference between revisions

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[[Image:1o7x.png|left|200px]]

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~~'''~~CITRATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS~~'''~~

===CITRATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS===

~~==Overview==~~

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The ~~crystal structure of citrate synthase from the thermophilic Archaeon Sulfolobus solfataricus (optimum growth temperature = 85 degrees C) has been determined~~, ~~extending~~ the ~~number of crystal structures of citrate synthase from different organisms~~ to ~~a total of five that span~~ the ~~temperature range over which life exists~~ (~~from psychrophile to hyperthermophile)~~. ~~Detailed structural analysis has revealed possible molecular mechanisms that determine the different stabilities of the five proteins~~. ~~The key to these mechanisms~~ is the precise structural location of the additional interactions. As one ascends the temperature ladder, the subunit interface of this dimeric enzyme and loop regions are reinforced by complex electrostatic interactions, and there is a reduced exposure of hydrophobic surface. These observations reveal a progressive pattern of stabilization through multiple additional interactions at solvent exposed, loop and interfacial regions.

The line below this paragraph, {{ABSTRACT_PUBMED_12473121}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12473121 is the PubMed ID number.

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==About this Structure==

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[[Category: Lyase]]

[[Category: Tricarboxylic acid cycle]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 03~~:29:58 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:25:11 2008''

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-[[Image:1o7x.jpg|left|200px]]
+{{Seed}}
+[[Image:1o7x.png|left|200px]]
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 {{STRUCTURE_1o7x|  PDB=1o7x  |  SCENE=  }}
-'''CITRATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS'''
+===CITRATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS===
-==Overview==
+<!--
-The crystal structure of citrate synthase from the thermophilic Archaeon Sulfolobus solfataricus (optimum growth temperature = 85 degrees C) has been determined, extending the number of crystal structures of citrate synthase from different organisms to a total of five that span the temperature range over which life exists (from psychrophile to hyperthermophile). Detailed structural analysis has revealed possible molecular mechanisms that determine the different stabilities of the five proteins. The key to these mechanisms is the precise structural location of the additional interactions. As one ascends the temperature ladder, the subunit interface of this dimeric enzyme and loop regions are reinforced by complex electrostatic interactions, and there is a reduced exposure of hydrophobic surface. These observations reveal a progressive pattern of stabilization through multiple additional interactions at solvent exposed, loop and interfacial regions.
+The line below this paragraph, {{ABSTRACT_PUBMED_12473121}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12473121 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12473121}}
 ==About this Structure==
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 [[Category: Lyase]]
 [[Category: Tricarboxylic acid cycle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:29:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:25:11 2008''