Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3--creatine transition-state analogue complex

Seoung Min Bong, Jin Ho Moon, Ki Hyun Nam, Ki Seog Lee, Young Min Chi, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

67 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3959-3965
Number of pages7
JournalFEBS Letters
Volume582
Issue number28
DOIs
Publication statusPublished - 2008 Nov 26

Bibliographical note

Funding Information:
We thank Drs. H.S. Lee, K.H. Kim, and K.J. Kim at Beam Line 4A, Pohang Accessory Laboratory, for assistance with the data collection. This experiment was supported by the Functional Proteomics Center, 21C Frontier Program of the Korea Ministry of Science and Technology.

Keywords

  • Brain-type creatine kinase
  • Creatine complex
  • Crystal structure
  • Energy homeostasis
  • Shuttle system

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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