2qrc: Difference between revisions

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[[Image:2qrc.~~jpg~~|left|200px]]

[[Image:2qrc.png|left|200px]]

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~~'''~~Crystal structure of the adenylate sensor from AMP-activated protein kinase in complex with ADP and AMP~~'''~~

===Crystal structure of the adenylate sensor from AMP-activated protein kinase in complex with ADP and AMP===

~~==Overview==~~

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The ~~AMP-activated protein kinase (AMPK)~~, ~~a sensor of cellular energy status found in all eukaryotes~~, ~~responds~~ to changes in intracellular adenosine nucleotide levels resulting from metabolic stresses. Here we describe crystal structures of a heterotrimeric regulatory core fragment from Schizosaccharomyces pombe AMPK in complex with ADP, ADP/~~AMP, ADP~~/~~ATP, and 5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranotide (AICAR phosphate, or ZMP), a well-characterized AMPK activator~~. ~~Prior crystallographic studies had revealed a single site in the gamma subunit that binds either ATP or AMP within Bateman domain B~~. ~~Here we show that ZMP binds at this site~~, ~~mimicking~~ the binding of AMP. An analogous site in Bateman domain A selectively accommodates ADP, which binds in a distinct manner that also involves direct ligation to elements from the beta subunit. These observations suggest a possible role for ADP in regulating AMPK response to changes in cellular energy status.

The line below this paragraph, {{ABSTRACT_PUBMED_17937917}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17937917 is the PubMed ID number.

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==About this Structure==

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[[Category: Serine/threonine-protein kinase]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 15~~:28:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:40:35 2008''

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-[[Image:2qrc.jpg|left|200px]]
+{{Seed}}
+[[Image:2qrc.png|left|200px]]
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 {{STRUCTURE_2qrc|  PDB=2qrc  |  SCENE=  }}
-'''Crystal structure of the adenylate sensor from AMP-activated protein kinase in complex with ADP and AMP'''
+===Crystal structure of the adenylate sensor from AMP-activated protein kinase in complex with ADP and AMP===
-==Overview==
+<!--
-The AMP-activated protein kinase (AMPK), a sensor of cellular energy status found in all eukaryotes, responds to changes in intracellular adenosine nucleotide levels resulting from metabolic stresses. Here we describe crystal structures of a heterotrimeric regulatory core fragment from Schizosaccharomyces pombe AMPK in complex with ADP, ADP/AMP, ADP/ATP, and 5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranotide (AICAR phosphate, or ZMP), a well-characterized AMPK activator. Prior crystallographic studies had revealed a single site in the gamma subunit that binds either ATP or AMP within Bateman domain B. Here we show that ZMP binds at this site, mimicking the binding of AMP. An analogous site in Bateman domain A selectively accommodates ADP, which binds in a distinct manner that also involves direct ligation to elements from the beta subunit. These observations suggest a possible role for ADP in regulating AMPK response to changes in cellular energy status.
+The line below this paragraph, {{ABSTRACT_PUBMED_17937917}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17937917 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17937917}}
 ==About this Structure==
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 [[Category: Serine/threonine-protein kinase]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:28:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:40:35 2008''