Journal
FEBS LETTERS
Volume 582, Issue 28, Pages 3959-3965Publisher
WILEY
DOI: 10.1016/j.febslet.2008.10.039
Keywords
Brain-type creatine kinase; Shuttle system; Energy homeostasis; Crystal structure; Creatine complex
Funding
- Functional Proteomics Center
- 21C Frontier Program of the Korea Ministry of Science and Technology
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Creatine kinase is a member of the phosphagen kinase family, which catalyzes the reversible phosphoryl transfer reaction that occurs between ATP and creatine to produce ADP and phosphocreatine. Here, three structural aspects of human-brain-type-creatine-kinase (hBB-CK) were identified by X-ray crystallography: the ligand-free-form at 2.2 angstrom; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0 angstrom. The structures of ligand-bound hBB-CK revealed two different monomeric states in a single homodimer. One monomer is a closed form, either bound to TSAC or the ADP-Mg2+-complex, and the second monomer is an unliganded open form. These structural studies provide a detailed mechanism indicating that the binding of ADP-Mg2+ alone may trigger conformational changes in hBB-CK that were not observed with muscle-type-CK. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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