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Title: Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase

Abstract

The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular adenosine triphosphate (ATP) and AMP levels. Here we report crystal structures at 2.6 and 2.9 Angstrom resolution for ATP- and AMP-bound forms of a core {alpha}{beta}{gamma} adenylate-binding domain from the fission yeast AMPK homologue. ATP and AMP bind competitively to a single site in the {gamma} subunit, with their respective phosphate groups positioned near function-impairing mutants. Surprisingly, ATP binds without counter ions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.

Authors:
;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930644
Report Number(s):
BNL-81064-2008-JA
Journal ID: ISSN 0193-4511; SCEHDK; TRN: US200901%%159
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Science; Journal Volume: 315
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; ADENOSINE; ATP; AVAILABILITY; CRYSTAL STRUCTURE; ELECTROSTATICS; FISSION; MUTANTS; PHOSPHATES; PHOSPHOTRANSFERASES; PROTEINS; RESOLUTION; YEASTS; national synchrotron light source

Citation Formats

Townley,R., and Shapiro, L.. Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase. United States: N. p., 2007. Web. doi:10.1126/science.1137503.
Townley,R., & Shapiro, L.. Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase. United States. doi:10.1126/science.1137503.
Townley,R., and Shapiro, L.. Mon . "Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase". United States. doi:10.1126/science.1137503.
@article{osti_930644,
title = {Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase},
author = {Townley,R. and Shapiro, L.},
abstractNote = {The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular adenosine triphosphate (ATP) and AMP levels. Here we report crystal structures at 2.6 and 2.9 Angstrom resolution for ATP- and AMP-bound forms of a core {alpha}{beta}{gamma} adenylate-binding domain from the fission yeast AMPK homologue. ATP and AMP bind competitively to a single site in the {gamma} subunit, with their respective phosphate groups positioned near function-impairing mutants. Surprisingly, ATP binds without counter ions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.},
doi = {10.1126/science.1137503},
journal = {Science},
number = ,
volume = 315,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}