Publication Date:
2007-02-10
Description:
The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 and 2.6 A resolution for ATP- and AMP-bound forms of a core alphabetagamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the gamma subunit, with their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, ATP binds without counterions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Townley, Robert -- Shapiro, Lawrence -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1726-9. Epub 2007 Feb 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289942" target="_blank"〉PubMed〈/a〉
Keywords:
AMP-Activated Protein Kinases
;
Adenosine Monophosphate/metabolism
;
Adenosine Triphosphate/metabolism
;
Amino Acid Sequence
;
Binding Sites
;
Binding, Competitive
;
Crystallization
;
Crystallography, X-Ray
;
Dimerization
;
Hydrogen Bonding
;
Hydrophobic and Hydrophilic Interactions
;
Models, Molecular
;
Molecular Sequence Data
;
Multienzyme Complexes/*chemistry/metabolism
;
Protein Kinases/*chemistry/metabolism
;
Protein Structure, Quaternary
;
Protein Structure, Tertiary
;
Protein Subunits/chemistry/metabolism
;
Protein-Serine-Threonine Kinases/*chemistry/metabolism
;
Schizosaccharomyces/*enzymology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
