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


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==MITOCHONDRIAL CREATINE KINASE==
The line below this paragraph, containing "STRUCTURE_1crk", creates the "Structure Box" on the page.
<StructureSection load='1crk' size='340' side='right'caption='[[1crk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1crk]] 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=1CRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRK FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
{{STRUCTURE_1crk| PDB=1crk |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1crk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1crk OCA], [https://pdbe.org/1crk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1crk RCSB], [https://www.ebi.ac.uk/pdbsum/1crk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1crk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KCRS_CHICK KCRS_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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cr/1crk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1crk ConSurf].
<div style="clear:both"></div>


'''MITOCHONDRIAL CREATINE KINASE'''
==See Also==
 
*[[Creatine Kinase|Creatine Kinase]]
 
*[[Creatine kinase 3D structures|Creatine kinase 3D structures]]
==Overview==
__TOC__
Creatine kinase (CK, EC 2.7.3.2), an enzyme important for energy metabolism in cells of high and fluctuating energy requirements, catalyses the reversible transfer of a phosphoryl goup from phosphocreatine to ADP. We have solved the structure of the octameric mitochondrial isoform, Mib-CK, which is located in the intermembrane compartment and along the cristae membranes. Mib-CK consumes ATP produced in the mitochondria for the production of phosphocreatine, which is then exported into the cytosol for fast regeneration of ATP by the cytosolic CK isoforms. The octamer has 422 point-group symmetry, and appears as a cube of side length 93 angstrom with a channel 20 angstrom wide extending along the four-fold axis. Positively charged amino acids at the four-fold faces of the octamer possibly interact with negatively charged mitochondrial membranes. Each monomer consists of a small alpha-helical domain and a large domain containing an eight-stranded antiparallel beta-sheet flanked by seven alpha-helices. The conserved residues of the CK family form a compact cluster that covers the active site between the domains.
</StructureSection>
 
==About this Structure==
1CRK 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=1CRK OCA].
 
==Reference==
Structure of mitochondrial creatine kinase., Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W, Nature. 1996 May 23;381(6580):341-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8692275 8692275]
[[Category: Creatine kinase]]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fritz-Wolf, K.]]
[[Category: Fritz-Wolf K]]
[[Category: Kabsch, W.]]
[[Category: Kabsch W]]
[[Category: Schnyder, T.]]
[[Category: Schnyder T]]
[[Category: Wallimann, T.]]
[[Category: Wallimann T]]
[[Category: Creatine kinase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:02:42 2008''

Latest revision as of 09:45, 7 February 2024

MITOCHONDRIAL CREATINE KINASEMITOCHONDRIAL CREATINE KINASE

Structural highlights

1crk is a 4 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCRS_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.

See Also

1crk, resolution 3.00Å

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