1ds5: Difference between revisions

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-[[Image:1ds5.gif|left|200px]]
- {{Structure
+==DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.==
-|PDB= 1ds5 |SIZE=350|CAPTION= <scene name='initialview01'>1ds5</scene>, resolution 3.16&Aring;
+<StructureSection load='1ds5' size='340' side='right'caption='[[1ds5]], [[Resolution|resolution]] 3.16&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
+<table><tr><td colspan='2'>[[1ds5]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DS5 FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.16&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1ds5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds5 OCA], [https://pdbe.org/1ds5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ds5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ds5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ds5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CSK2A_MAIZE CSK2A_MAIZE] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
+== 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/ds/1ds5_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=1ds5 ConSurf].
+<div style="clear:both"></div>
-'''DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.'''
+==See Also==
+*[[Casein kinase 3D structures|Casein kinase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The crystal structure of a complex between the catalytic alpha subunit of Zea mays CK2 and a 23-mer peptide corresponding the C-terminal sequence 181-203 of the human CK2 regulatory beta subunit has been determined at 3.16-A resolution. The complex, composed of two alpha chains and two peptides, presents a molecular twofold axis, with each peptide interacting with both alpha chains. In the derived model of the holoenzyme, the regulatory subunits are positioned on the opposite side with respect to the opening of the catalytic sites, that remain accessible to substrates and cosubstrates. The beta subunit can influence the catalytic activity both directly and by promoting the formation of the alpha2 dimer, in which each alpha chain interacts with the active site of the other. Furthermore, the two active sites are so close in space that they can simultaneously bind and phosphorylate two phosphoacceptor residues of the same substrate.
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
-==About this Structure==
-DS5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS5 OCA].
-==Reference==
-The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme., Battistutta R, Sarno S, De Moliner E, Marin O, Issinger OG, Zanotti G, Pinna LA, Eur J Biochem. 2000 Aug;267(16):5184-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10931203 10931203]
-[[Category: Non-specific serine/threonine protein kinase]]
-[[Category: Protein complex]]
 [[Category: Zea mays]]
-[[Category: Battistutta, R.]]
+[[Category: Battistutta R]]
-[[Category: Marin, O.]]
+[[Category: De Moliner E]]
-[[Category: Moliner, E De.]]
+[[Category: Marin O]]
-[[Category: Pinna, L A.]]
+[[Category: Pinna LA]]
-[[Category: Sarno, S.]]
+[[Category: Sarno S]]
-[[Category: Zanotti, G.]]
+[[Category: Zanotti G]]
-[[Category: AMP]]
-[[Category: MG]]
-[[Category: protein-complex]]
-[[Category: tetramer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:43:24 2008''