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Structure. 2011 Apr 13;19(4):515-22. doi: 10.1016/j.str.2011.01.018.

Structural insights into the architecture and allostery of full-length AMP-activated protein kinase.

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1
MOE Key Laboratory of Arid and Grassland Ecology, Institute of Biophysics, Lanzhou University, Lanzhou 730000, P.R. China.

Abstract

AMP-activated protein kinase (AMPK) is a heterotrimeric complex composed of α catalytic subunit, β scaffolding subunit, and γ regulatory subunit with critical roles in maintaining cellular energy homeostasis. However, the molecular architecture of the intact complex and the allostery associated with the adenosine binding-induced regulation of kinase activity remain unclear. Here, we determine the three-dimensional reconstruction and subunit organization of the full-length rat AMPK (α1β1γ1) through single-particle electron-microscopy. By comparing the structures of AMPK in ATP- and AMP-bound states, we are able to visualize the sequential conformational changes underlying kinase activation that transmits from the adenosine binding sites in the γ subunit to the kinase domain of the α subunit. These results not only make substantial revision to the current model of AMPK assembly, but also highlight a central role of the linker sequence of the α subunit in mediating the allostery of AMPK.

PMID:
21481774
DOI:
10.1016/j.str.2011.01.018
[Indexed for MEDLINE]
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