2qrc
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2qrc.jpg|left|200px]] | [[Image:2qrc.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2qrc", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{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''' | ||
Line 29: | Line 26: | ||
[[Category: Shapiro, L.]] | [[Category: Shapiro, L.]] | ||
[[Category: Townley, R.]] | [[Category: Townley, R.]] | ||
- | [[Category: | + | [[Category: Adp]] |
- | [[Category: | + | [[Category: Amp]] |
- | [[Category: | + | [[Category: Ampk]] |
- | [[Category: | + | [[Category: Atp-binding]] |
- | [[Category: | + | [[Category: Cbs domain]] |
- | [[Category: | + | [[Category: Kinase]] |
- | [[Category: | + | [[Category: Nucleotide-binding]] |
- | [[Category: | + | [[Category: Serine/threonine-protein kinase]] |
- | [[Category: | + | [[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 | + |
Revision as of 12:28, 4 May 2008
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.
About this Structure
2QRC is a Protein complex structure of sequences from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
Reference
Structural insight into AMPK regulation: ADP comes into play., Jin X, Townley R, Shapiro L, Structure. 2007 Oct;15(10):1285-95. PMID:17937917 Page seeded by OCA on Sun May 4 15:28:54 2008