3TE5
structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH
Summary for 3TE5
| Entry DOI | 10.2210/pdb3te5/pdb |
| Related | 3TDH |
| Descriptor | Carbon catabolite-derepressing protein kinase, SNF1 protein kinase subunit beta-2, Nuclear protein SNF4, ... (5 entities in total) |
| Functional Keywords | cbs domain, nucleotide binding, cytosol, transferase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Nucleus membrane; Peripheral membrane protein: P06782 Cytoplasm: P34164 Nucleus: P12904 |
| Total number of polymer chains | 3 |
| Total formula weight | 70668.23 |
| Authors | Mayer, F.V.,Heath, R.,Underwood, E.,Sanders, M.J.,Carmena, D.,McCartney, R.,Leiper, F.C.,Xiao, B.,Jing, C.,Walker, P.A.,Haire, L.F.,Ogrodowicz, R.,Martin, S.R.,Schmidt, M.C.,Gamblin, S.J.,Carling, D. (deposition date: 2011-08-12, release date: 2011-11-09, Last modification date: 2024-02-28) |
| Primary citation | Mayer, F.V.,Heath, R.,Underwood, E.,Sanders, M.J.,Carmena, D.,McCartney, R.R.,Leiper, F.C.,Xiao, B.,Jing, C.,Walker, P.A.,Haire, L.F.,Ogrodowicz, R.,Martin, S.R.,Schmidt, M.C.,Gamblin, S.J.,Carling, D. ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase. Cell Metab, 14:707-714, 2011 Cited by PubMed Abstract: The SNF1 protein kinase complex plays an essential role in regulating gene expression in response to the level of extracellular glucose in budding yeast. SNF1 shares structural and functional similarities with mammalian AMP-activated protein kinase. Both kinases are activated by phosphorylation on a threonine residue within the activation loop segment of the catalytic subunit. Here we show that ADP is the long-sought metabolite that activates SNF1 in response to glucose limitation by protecting the enzyme against dephosphorylation by Glc7, its physiologically relevant protein phosphatase. We also show that the regulatory subunit of SNF1 has two ADP binding sites. The tighter site binds AMP, ADP, and ATP competitively with NADH, whereas the weaker site does not bind NADH, but is responsible for mediating the protective effect of ADP on dephosphorylation. Mutagenesis experiments suggest that the general mechanism by which ADP protects against dephosphorylation is strongly conserved between SNF1 and AMPK. PubMed: 22019086DOI: 10.1016/j.cmet.2011.09.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
