1qh4: Difference between revisions
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[[Image:1qh4.gif|left|200px]] | [[Image:1qh4.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION''' | {{Structure | ||
|PDB= 1qh4 |SIZE=350|CAPTION= <scene name='initialview01'>1qh4</scene>, resolution 1.41Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | |||
|ACTIVITY= [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] | |||
|GENE= EMBL-NR. X03509 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | |||
}} | |||
'''CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QH4 is a [ | 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== | ==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:// | 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: Creatine kinase]] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
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[[Category: cellular energy metabolism]] | [[Category: cellular energy metabolism]] | ||
[[Category: guanidino kinase]] | [[Category: guanidino kinase]] | ||
[[Category: neurodegenerative | [[Category: neurodegenerative disorder]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:37:23 2008'' | ||
Revision as of 14:37, 20 March 2008
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| , resolution 1.41Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | EMBL-NR. X03509 (Gallus gallus) | ||||||
| Activity: | Creatine kinase, with EC number 2.7.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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