1qh4: Difference between revisions
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'''CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION''' | '''CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION''' | ||
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[[Category: Schlattner, U.]] | [[Category: Schlattner, U.]] | ||
[[Category: Wallimann, T.]] | [[Category: Wallimann, T.]] | ||
[[Category: | [[Category: Brain-type creatine kinase]] | ||
[[Category: | [[Category: Cancer]] | ||
[[Category: | [[Category: Cellular energy metabolism]] | ||
[[Category: | [[Category: Guanidino kinase]] | ||
[[Category: | [[Category: Neurodegenerative disorder]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:15:54 2008'' | |||
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Revision as of 06:15, 3 May 2008
CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION
OverviewOverview
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.
About this StructureAbout this Structure
1QH4 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
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. 1999 Nov;8(11):2258-69. PMID:10595529 Page seeded by OCA on Sat May 3 06:15:54 2008