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| | <StructureSection load='1qh4' size='340' side='right'caption='[[1qh4]], [[Resolution|resolution]] 1.41Å' scene=''> | | <StructureSection load='1qh4' size='340' side='right'caption='[[1qh4]], [[Resolution|resolution]] 1.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qh4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QH4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qh4]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QH4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.41Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EMBL-NR. X03509 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Creatine_kinase Creatine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.2 2.7.3.2] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qh4 OCA], [https://pdbe.org/1qh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qh4 RCSB], [https://www.ebi.ac.uk/pdbsum/1qh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qh4 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qh4 OCA], [https://pdbe.org/1qh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qh4 RCSB], [https://www.ebi.ac.uk/pdbsum/1qh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qh4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/KCRB_CHICK KCRB_CHICK]] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
| + | [https://www.uniprot.org/uniprot/KCRB_CHICK KCRB_CHICK] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Creatine kinase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, A]] | + | [[Category: Becker A]] |
| - | [[Category: Eder, M]] | + | [[Category: Eder M]] |
| - | [[Category: Fritz-Wolf, K]] | + | [[Category: Fritz-Wolf K]] |
| - | [[Category: Kabsch, W]] | + | [[Category: Kabsch W]] |
| - | [[Category: Schlattner, U]] | + | [[Category: Schlattner U]] |
| - | [[Category: Wallimann, T]] | + | [[Category: Wallimann T]] |
| - | [[Category: Brain-type creatine kinase]]
| + | |
| - | [[Category: Cancer]]
| + | |
| - | [[Category: Cellular energy metabolism]]
| + | |
| - | [[Category: Guanidino kinase]]
| + | |
| - | [[Category: Neurodegenerative disorder]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
KCRB_CHICK Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 1999 Nov;8(11):2258-69. PMID:10595529
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