AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

Lei Chen; Jue Wang; Yuan-Yuan Zhang; S Frank Yan; Dietbert Neumann; Uwe Schlattner; Zhi-Xin Wang; Jia-Wei Wu

doi:10.1038/nsmb.2319

AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

Nat Struct Mol Biol. 2012 Jun 3;19(7):716-8. doi: 10.1038/nsmb.2319.

Authors

Lei Chen¹, Jue Wang, Yuan-Yuan Zhang, S Frank Yan, Dietbert Neumann, Uwe Schlattner, Zhi-Xin Wang, Jia-Wei Wu

Affiliation

¹ MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.

PMID: 22659875
DOI: 10.1038/nsmb.2319

Abstract

The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the γ subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the γ subunit in the presence of ATP. However, site 3 is occupied in the presence of AMP. Mutagenesis studies indicate that sites 3 and 4 are important for AMPK allosteric activation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

AMP-Activated Protein Kinases / chemistry
AMP-Activated Protein Kinases / metabolism*
Adenine Nucleotides / metabolism*
Allosteric Regulation
Protein Conformation

Substances

Adenine Nucleotides
AMP-Activated Protein Kinases

Associated data

PDB/4EAG
PDB/4EAI
PDB/4EAJ
PDB/4EAK
PDB/4EAL