Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex |
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Authors: | Bong Seoung Min Moon Jin Ho Nam Ki Hyun Lee Ki Seog Chi Young Min Hwang Kwang Yeon |
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Institution: | Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea |
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Abstract: | 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 Å; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0 Å. 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. |
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Keywords: | Brain-type creatine kinase Shuttle system Energy homeostasis Crystal structure Creatine complex |
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