1bl5: Difference between revisions

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[[Image:1bl5.~~gif~~|left|200px]]

[[Image:1bl5.png|left|200px]]

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~~'''~~ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION~~'''~~

===ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION===

~~==Overview==~~

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The structure of a rate-limited product complex formed during a single initial round of turnover by isocitrate dehydrogenase has been determined. Photolytic liberation of either caged substrate or caged cofactor and Laue X-ray data collection were used to visualize the complex, ~~which has a minimum half-life of approximately 10 milliseconds. The experiment was conducted with three different photoreactive compounds~~, ~~each possessing a unique mechanism leading~~ to the ~~formation of the enzyme-substrate~~ (~~ES) complex~~. ~~Photoreaction efficiency and subsequent substrate affinities and binding rates in the crystal are critical parameters for these experiments~~. ~~The structure suggests that CO2 dissociation~~ is ~~a rapid event that may help drive product formation, and that small conformational changes may contribute to slow product release~~.

The line below this paragraph, {{ABSTRACT_PUBMED_9783749}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9783749 is the PubMed ID number.

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==About this Structure==

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[[Category: Oxidoreductase]]

[[Category: Phosphorylation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:39:18 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:20:01 2008''

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-[[Image:1bl5.gif|left|200px]]
+{{Seed}}
+[[Image:1bl5.png|left|200px]]
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 {{STRUCTURE_1bl5|  PDB=1bl5  |  SCENE=  }}
-'''ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION'''
+===ISOCITRATE DEHYDROGENASE FROM E. COLI SINGLE TURNOVER LAUE STRUCTURE OF RATE-LIMITED PRODUCT COMPLEX, 10 MSEC TIME RESOLUTION===
-==Overview==
+<!--
-The structure of a rate-limited product complex formed during a single initial round of turnover by isocitrate dehydrogenase has been determined. Photolytic liberation of either caged substrate or caged cofactor and Laue X-ray data collection were used to visualize the complex, which has a minimum half-life of approximately 10 milliseconds. The experiment was conducted with three different photoreactive compounds, each possessing a unique mechanism leading to the formation of the enzyme-substrate (ES) complex. Photoreaction efficiency and subsequent substrate affinities and binding rates in the crystal are critical parameters for these experiments. The structure suggests that CO2 dissociation is a rapid event that may help drive product formation, and that small conformational changes may contribute to slow product release.
+The line below this paragraph, {{ABSTRACT_PUBMED_9783749}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9783749 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9783749}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Phosphorylation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:39:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:20:01 2008''