2OOX
Crystal structure of the adenylate sensor from AMP-activated protein kinase complexed with AMP
Summary for 2OOX
| Entry DOI | 10.2210/pdb2oox/pdb |
| Related | 2OOY |
| Descriptor | SNF1-like protein kinase ssp2, SPCC1919.03c protein, Hypothetical protein C1556.08c in chromosome I, ... (5 entities in total) |
| Functional Keywords | ampk, kinase, amp, transferase |
| Biological source | Schizosaccharomyces pombe (fission yeast) More |
| Cellular location | Cytoplasm: P78789 |
| Total number of polymer chains | 6 |
| Total formula weight | 128961.94 |
| Authors | Townley, R.,Shapiro, L. (deposition date: 2007-01-26, release date: 2007-02-06, Last modification date: 2023-12-27) |
| Primary citation | Townley, R.,Shapiro, L. Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase. Science, 315:1726-1729, 2007 Cited by PubMed Abstract: The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 and 2.6 A resolution for ATP- and AMP-bound forms of a core alphabetagamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the gamma subunit, with their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, ATP binds without counterions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge. PubMed: 17289942DOI: 10.1126/science.1137503 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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