1lpu: Difference between revisions

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{{Seed}}
[[Image:1lpu.png|left|200px]]


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==Low Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays==
The line below this paragraph, containing "STRUCTURE_1lpu", creates the "Structure Box" on the page.
<StructureSection load='1lpu' size='340' side='right'caption='[[1lpu]], [[Resolution|resolution]] 1.86&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'>[[1lpu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LPU 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]] 1.86&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene></td></tr>
{{STRUCTURE_1lpu|  PDB=1lpu  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpu OCA], [https://pdbe.org/1lpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lpu RCSB], [https://www.ebi.ac.uk/pdbsum/1lpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpu 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/lp/1lpu_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=1lpu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein kinase CK2 (casein kinase 2) is a highly conserved and ubiquitously found eukaryotic serine/threonine kinase that plays a role in various cellular key processes like proliferation, apoptosis and circadian rhythm. One of its prominent biochemical properties is its ability to use GTP as well as ATP as a cosubstrate (dual-cosubstrate specificity). This feature is exceptional among eukaryotic protein kinases, and its biological significance is unknown. We describe here a mutant of the catalytic subunit of protein kinase CK2 (CK2alpha) from Homo sapiens (hsCK2alpha) with a clear and CK2-atypical preference for ATP compared to GTP. This mutant was designed on the basis of several structures of CK2alpha from Zea mays (zmCK2alpha) in complex with various ATP-competitive ligands. A structural overlay revealed the existence of a "purine base binding plane" harbouring the planar moiety of the respective ligand like the purine base of ATP and GTP. This purine base binding plane is sandwiched between the side-chains of Ile66 (Val66 in hsCK2alpha) and Met163, and it adopts a significantly different orientation than in prominent homologues like cAMP-dependent protein kinase (CAPK). By exchanging these two flanking amino acids (Val66Ala, Met163Leu) in hsCK2alpha(1-335), a C-terminally truncated variant of hsCK2alpha, the cosubstrate specificity shifted in the expected direction so that the mutant strongly favours ATP. A structure determination of the mutant in complex with an ATP-analogue confirmed the predicted change of the purine base binding plane orientation. An unexpected but in retrospect plausible consequence of the mutagenesis was, that the helix alpha D region, which is in the direct neighbourhood of the ATP-binding site, has adopted a conformation that is more similar to CAPK and less favourable for binding of GTP. These findings demonstrate that CK2alpha possesses sophisticated structural adaptations in favour of dual-cosubstrate specificity, suggesting that this property could be of biological significance.


===Low Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays===
Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.,Yde CW, Ermakova I, Issinger OG, Niefind K J Mol Biol. 2005 Mar 25;347(2):399-414. Epub 2005 Jan 18. PMID:15740749<ref>PMID:15740749</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lpu" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15740749}}, adds the Publication Abstract to the page
*[[Casein kinase 3D structures|Casein kinase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15740749 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15740749}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1LPU is a [[Single protein]] structure of sequence 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=1LPU OCA].
 
==Reference==
Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate., Yde CW, Ermakova I, Issinger OG, Niefind K, J Mol Biol. 2005 Mar 25;347(2):399-414. Epub 2005 Jan 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15740749 15740749]
 
Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution., Niefind K, Guerra B, Pinna LA, Issinger OG, Schomburg D, EMBO J. 1998 May 1;17(9):2451-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9564028 9564028]
 
Expression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Zea mays., Guerra B, Niefind K, Pinna LA, Schomburg D, Issinger OG, Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):143-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9761839 9761839]
 
GTP plus water mimic ATP in the active site of protein kinase CK2., Niefind K, Putter M, Guerra B, Issinger OG, Schomburg D, Nat Struct Biol. 1999 Dec;6(12):1100-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10581548 10581548]
 
Crystallization and preliminary characterization of crystals of human protein kinase CK2., Niefind K, Guerra B, Ermakowa I, Issinger OG, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1680-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11092945 11092945]
 
Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme., Niefind K, Guerra B, Ermakowa I, Issinger OG, EMBO J. 2001 Oct 1;20(19):5320-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11574463 11574463]
 
Expression and characterization of a recombinant maize CK-2 alpha subunit., Boldyreff B, Meggio F, Dobrowolska G, Pinna LA, Issinger OG, Biochim Biophys Acta. 1993 Apr 29;1173(1):32-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8485151 8485151]
 
Cloning and sequencing of the casein kinase 2 alpha subunit from Zea mays., Dobrowolska G, Boldyreff B, Issinger OG, Biochim Biophys Acta. 1991 Dec 2;1129(1):139-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1756176 1756176]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Single protein]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Guerra, B.]]
[[Category: Guerra B]]
[[Category: Issinger, O G.]]
[[Category: Issinger O-G]]
[[Category: Niefind, K.]]
[[Category: Niefind K]]
[[Category: Puetter, M.]]
[[Category: Puetter M]]
[[Category: Schomburg, D.]]
[[Category: Schomburg D]]
[[Category: Casein kinase 2]]
[[Category: Ck2]]
[[Category: Dual-cosubstrate specificity]]
[[Category: Protein kinase]]
 
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Retrieved from "https://proteopedia.org/1lpu"