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Crystal structure of brain-type creatine kinase at 1.41 A resolution.

Eder M, Schlattner U, Becker A, Wallimann T, Kabsch W, Fritz-Wolf K
Protein Sci 8 2258-69 (1999)
Cited: 64 times
EuropePMC logo PMID: 10595529

Abstract

Excitable cells and tissues like muscle or brain show a highly fluctuating consumption of ATP, which is efficiently regenerated from a large pool of phosphocreatine by the enzyme creatine kinase (CK). The enzyme exists in tissue--as well as compartment-specific isoforms. Numerous pathologies are related to the CK system: CK is found to be overexpressed in a wide range of solid tumors, whereas functional impairment of CK leads to a deterioration in energy metabolism, which is phenotypic for many neurodegenerative and age-related diseases. The crystal structure of chicken cytosolic brain-type creatine kinase (BB-CK) has been solved to 1.41 A resolution by molecular replacement. It represents the most accurately determined structure in the family of guanidino kinases. Except for the N-terminal region (2-12), the structures of both monomers in the biological dimer are very similar and closely resemble those of the other known structures in the family. Specific Ca2+-mediated interactions, found between two dimers in the asymmetric unit, result in structurally independent heterodimers differing in their N-terminal conformation and secondary structure. The high-resolution structure of BB-CK presented in this work will assist in designing new experiments to reveal the molecular basis of the multiple isoform-specific properties of CK, especially regarding different subcellular locations and functional interactions with other proteins. The rather similar fold shared by all known guanidino kinase structures suggests a model for the transition state complex of BB-CK analogous to the one of arginine kinase (AK). Accordingly, we have modeled a putative conformation of CK in the transition state that requires a rigid body movement of the entire N-terminal domain by rms 4 A from the structure without substrates.

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Related citations provided by authors (2)

  1. Transition State Structure of Arginine Kinase: Implications for Catalysis of Bimolecular Reactions. Zhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS Proc. Natl. Acad. Sci. U.S.A. 95 8449-8454 (1998)
  2. Structure of Mitochondrial Creatine Kinase.. Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W Nature 381 341-345 (1996)

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