2NYC
Crystal structure of the Bateman2 domain of yeast Snf4
Summary for 2NYC
| Entry DOI | 10.2210/pdb2nyc/pdb |
| Related | 2NYE |
| Descriptor | Nuclear protein SNF4 (2 entities in total) |
| Functional Keywords | bateman2 domain, snf4, amp kinase, protein binding |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus : P12904 |
| Total number of polymer chains | 1 |
| Total formula weight | 16174.68 |
| Authors | Rudolph, M.J.,Amodeo, G.A.,Iram, S.,Hong, S.,Pirino, G.,Carlson, M.,Tong, L. (deposition date: 2006-11-20, release date: 2006-12-12, Last modification date: 2023-12-27) |
| Primary citation | Rudolph, M.J.,Amodeo, G.A.,Iram, S.,Hong, S.P.,Pirino, G.,Carlson, M.,Tong, L. Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding. Structure, 15:65-74, 2007 Cited by PubMed Abstract: AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. AMP is believed to control the activity of AMPK by binding to the gamma subunit of this heterotrimeric enzyme. This subunit contains two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. No structural information is currently available on this subunit, and the molecular basis for its interactions with AMP is not well understood. We report here the crystal structure at 1.9 Angstrom resolution of the Bateman2 domain of Snf4, the gamma subunit of the yeast ortholog of AMPK. The structure revealed a dimer of the Bateman2 domain, and this dimerization is supported by our light-scattering, mutagenesis, and biochemical studies. There is a prominent pocket at the center of this dimer, and most of the disease-causing mutations are located in or near this pocket. PubMed: 17223533DOI: 10.1016/j.str.2006.11.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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