2fh9
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= SNF1, CAT1, CCR1, GLC2, PAS14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= SNF1, CAT1, CCR1, GLC2, PAS14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh9 OCA], [http://www.ebi.ac.uk/pdbsum/2fh9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fh9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nayak, V.]] | [[Category: Nayak, V.]] | ||
| - | [[Category: kinase domain | + | [[Category: dimer]] |
| + | [[Category: kinase domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:02:44 2008'' |
Revision as of 00:02, 31 March 2008
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| , resolution 2.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | SNF1, CAT1, CCR1, GLC2, PAS14 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure and dimerization of the kinase domain from yeast Snf1
Overview
The Snf1/AMPK kinases are intracellular energy sensors, and the AMPK pathway has been implicated in a variety of metabolic human disorders. Here we report the crystal structure of the kinase domain from yeast Snf1, revealing a bilobe kinase fold with greatest homology to cyclin-dependant kinase-2. Unexpectedly, the crystal structure also reveals a novel homodimer that we show also forms in solution, as demonstrated by equilibrium sedimentation, and in yeast cells, as shown by coimmunoprecipitation of differentially tagged intact Snf1. A mapping of sequence conservation suggests that dimer formation is a conserved feature of the Snf1/AMPK kinases. The conformation of the conserved alphaC helix, and the burial of the activation segment and substrate binding site within the dimer, suggests that it represents an inactive form of the kinase. Taken together, these studies suggest another layer of kinase regulation within the Snf1/AMPK family, and an avenue for development of AMPK-specific activating compounds.
About this Structure
2FH9 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family., Nayak V, Zhao K, Wyce A, Schwartz MF, Lo WS, Berger SL, Marmorstein R, Structure. 2006 Mar;14(3):477-85. PMID:16531232
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