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Structural studies of human brain‐type creatine kinase complexed with the ADP–Mg 2+ –NO 3− –creatine transition‐state analogue complex
Author(s) -
Bong Seoung Min,
Moon Jin Ho,
Nam Ki Hyun,
Lee Ki Seog,
Chi Young Min,
Hwang Kwang Yeon
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.10.039
Subject(s) - phosphocreatine , creatine kinase , creatine , chemistry , monomer , transition state analog , stereochemistry , ligand (biochemistry) , crystallography , enzyme , biochemistry , active site , biology , receptor , endocrinology , polymer , organic chemistry , energy metabolism
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 ( h BB‐CK) were identified by X‐ray crystallography: the ligand‐free‐form at 2.2 Å; the ADP–Mg 2+ , nitrate, and creatine complex (transition‐state‐analogue complex; TSAC); and the ADP–Mg 2+ ‐complex at 2.0 Å. The structures of ligand‐bound h BB‐CK revealed two different monomeric states in a single homodimer. One monomer is a closed form, either bound to TSAC or the ADP–Mg 2+ ‐complex, and the second monomer is an unliganded open form. These structural studies provide a detailed mechanism indicating that the binding of ADP–Mg 2+ alone may trigger conformational changes in h BB‐CK that were not observed with muscle‐type‐CK.