1QH4

CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION

Summary for 1QH4

• Entry DOI: 10.2210/pdb1qh4/pdb
• Descriptor: CREATINE KINASE, ACETATE ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: brain-type creatine kinase, cancer, cellular energy metabolism, guanidino kinase, neurodegenerative disorders, transferase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 4
• Total formula weight: 171592.43

Authors

Eder, M.,Schlattner, U.,Becker, A.,Wallimann, T.,Kabsch, W.,Fritz-Wolf, K. (deposition date: 1999-05-11, release date: 1999-11-19, Last modification date: 2023-08-16)

Primary citation

Eder, M.,Schlattner, U.,Becker, A.,Wallimann, T.,Kabsch, W.,Fritz-Wolf, K.
Crystal structure of brain-type creatine kinase at 1.41 A resolution.
Protein Sci., 8:2258-2269, 1999

PubMed 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.

PubMed: 10595529

Experimental method

X-RAY DIFFRACTION (1.41 Å)