View source for 1qh4

[[Image:1qh4.gif|left|200px]]

 {{Structure
|PDB= 1qh4 |SIZE=350|CAPTION= <scene name='initialview01'>1qh4</scene>, resolution 1.41&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatine_kinase Creatine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.2 2.7.3.2] </span>
|GENE= EMBL-NR. X03509 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qh4 OCA], [http://www.ebi.ac.uk/pdbsum/1qh4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qh4 RCSB]</span>
}}

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


==Overview==
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 Structure==
1QH4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH4 OCA]. 

==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10595529 10595529]
[[Category: Creatine kinase]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Becker, A.]]
[[Category: Eder, M.]]
[[Category: Fritz-Wolf, K.]]
[[Category: Kabsch, W.]]
[[Category: Schlattner, U.]]
[[Category: Wallimann, T.]]
[[Category: brain-type creatine kinase]]
[[Category: cancer]]
[[Category: cellular energy metabolism]]
[[Category: guanidino kinase]]
[[Category: neurodegenerative disorder]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:13:29 2008''