2FH9
Structure and dimerization of the kinase domain from yeast Snf1
Summary for 2FH9
| Entry DOI | 10.2210/pdb2fh9/pdb |
| Descriptor | Snf1 kinase (2 entities in total) |
| Functional Keywords | kinase domain; dimer, signaling protein, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasm : P06782 |
| Total number of polymer chains | 1 |
| Total formula weight | 31255.40 |
| Authors | Nayak, V. (deposition date: 2005-12-23, release date: 2006-03-28, Last modification date: 2024-02-14) |
| Primary citation | Nayak, V.,Zhao, K.,Wyce, A.,Schwartz, M.F.,Lo, W.S.,Berger, S.L.,Marmorstein, R. Structure and Dimerization of the Kinase Domain from Yeast Snf1, a Member of the Snf1/AMPK Protein Family Structure, 14:477-485, 2006 Cited by PubMed Abstract: 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. PubMed: 16531232DOI: 10.1016/j.str.2005.12.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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