3B6R

Crystal structure of Human Brain-type Creatine Kinase

Summary for 3B6R

• Entry DOI: 10.2210/pdb3b6r/pdb
• Descriptor: Creatine kinase B-type, ACETATE ION, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: brain type, dimeric, atp-binding, cytoplasm, kinase, nucleotide-binding, phosphorylation, polymorphism, transferase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: P12277
• Total number of polymer chains: 2
• Total formula weight: 86161.15

Authors

Bong, S.M.,Moon, J.H.,Hwang, K.Y. (deposition date: 2007-10-29, release date: 2008-11-04, Last modification date: 2023-11-01)

Primary citation

Bong, S.M.,Moon, J.H.,Nam, K.H.,Lee, K.S.,Chi, Y.M.,Hwang, K.Y.
Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex
Febs Lett., 582:3959-3965, 2008

PubMed 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 2.2A; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0A. 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.

PubMed: 18977227
DOI: 10.1016/j.febslet.2008.10.039

Experimental method

X-RAY DIFFRACTION (2 Å)