Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase

被引：151

作者：

Townley, Robert

Shapiro, Lawrence ^{[1
]}

机构：

[1] Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10032 USA

[2] Columbia Univ, Edward S Harkness Eye Inst, New York, NY 10032 USA

[3] Columbia Univ, Naomi Berrie Diabet Ctr, New York, NY 10032 USA

来源：

SCIENCE | 2007年 / 315卷 / 5819期

关键词：

D O I：

10.1126/science.1137503

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 angstrom resolution for ATP- and AMP-bound forms of a core alpha beta gamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the g 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.

引用

页码：1726 / 1729

页数：4

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