Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase
Robert Townley1 and
Lawrence Shapiro1,2,3*
The 5'-AMP (adenosine monophosphate)–activated proteinkinase (AMPK) coordinates metabolic function with energy availabilityby responding to changes in intracellular ATP (adenosine triphosphate)and AMP concentrations. Here, we report crystal structures at2.9 and 2.6 Å resolution for ATP- and AMP-bound formsof a core ß adenylate-binding domain from the fissionyeast AMPK homolog. ATP and AMP bind competitively to a singlesite in the subunit, with their respective phosphate groupspositioned near function-impairing mutants. Unexpectedly, ATPbinds without counterions, amplifying its electrostatic effectson a critical regulatory region where all three subunits converge.
1 Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. 2 Edward S. Harkness Eye Institute, Columbia University, New York, NY 10032, USA. 3 Naomi Berrie Diabetes Center, Columbia University, New York, NY 10032, USA.
* To whom correspondence should be addressed. E-mail: LSS8{at}columbia.edu
Roles of the Glycogen-binding Domain and Snf4 in Glucose Inhibition of SNF1 Protein Kinase.
M. Momcilovic, S. H. Iram, Y. Liu, and M. Carlson (2008)
J. Biol. Chem.
283, 19521-19529
|Abstract »|Full Text »|PDF »
Structural Properties of AMP-activated Protein Kinase: DIMERIZATION, MOLECULAR SHAPE, AND CHANGES UPON LIGAND BINDING.
U. Riek, R. Scholz, P. Konarev, A. Rufer, M. Suter, A. Nazabal, P. Ringler, M. Chami, S. A. Muller, D. Neumann, et al. (2008)
J. Biol. Chem.
283, 18331-18343
|Abstract »|Full Text »|PDF »
Minireview: Adenosine 5'-Monophosphate-Activated Protein Kinase Regulation of Fatty Acid Oxidation in Skeletal Muscle.
AMP-activated Protein Kinase Subunit Interactions: {beta}1:{gamma}1 ASSOCIATION REQUIRES {beta}1 Thr-263 AND Tyr-267.
T. J. Iseli, J. S. Oakhill, M. F. Bailey, S. Wee, M. Walter, B. J. van Denderen, L. A. Castelli, F. Katsis, L. A. Witters, D. Stapleton, et al. (2008)
J. Biol. Chem.
283, 4799-4807
|Abstract »|Full Text »|PDF »
5'-AMP-Activated Protein Kinase Signaling in Caenorhabditis elegans.
Inhibition of Skeletal Muscle ClC-1 Chloride Channels by Low Intracellular pH and ATP.
B. Bennetts, M. W. Parker, and B. A. Cromer (2007)
J. Biol. Chem.
282, 32780-32791
|Abstract »|Full Text »|PDF »
Defining the Mechanism of Activation of AMP-activated Protein Kinase by the Small Molecule A-769662, a Member of the Thienopyridone Family.
M. J. Sanders, Z. S. Ali, B. D. Hegarty, R. Heath, M. A. Snowden, and D. Carling (2007)
J. Biol. Chem.
282, 32539-32548
|Abstract »|Full Text »|PDF »
A Conserved Sequence Immediately N-terminal to the Bateman Domains in AMP-activated Protein Kinase {gamma} Subunits Is Required for the Interaction with the beta Subunits.
R. Viana, M. C. Towler, D. A. Pan, D. Carling, B. Viollet, D. G. Hardie, and P. Sanz (2007)
J. Biol. Chem.
282, 16117-16125
|Abstract »|Full Text »|PDF »
ß
adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the 
