Detail Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase   Oleh:  Townley, Robert ; Shapiro, Lawrence E. Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 315 no. 5819 (Mar. 2007), page 1726. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.03 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel 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 al3Y adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the y 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. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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