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-Structure paper
タイトル | Structural insights into the architecture and allostery of full-length AMP-activated protein kinase. |
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ジャーナル・号・ページ | Structure, Vol. 19, Issue 4, Page 515-522, Year 2011 |
掲載日 | 2011年4月13日 |
著者 | Li Zhu / Lei Chen / Xiao-Ming Zhou / Yuan-Yuan Zhang / Yi-Jiong Zhang / Jing Zhao / Shang-Rong Ji / Jia-Wei Wu / Yi Wu / |
PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:21481774 |
手法 | EM (単粒子) |
解像度 | 19.0 - 20.0 Å |
構造データ | EMDB-1897: EMDB-1898: EMDB-1899: |
由来 |
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