1ds5: Difference between revisions

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New page: left|200px<br /> <applet load="1ds5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ds5, resolution 3.16Å" /> '''DIMERIC CRYSTAL STR...
 
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[[Image:1ds5.gif|left|200px]]<br />
<applet load="1ds5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ds5, resolution 3.16&Aring;" />
'''DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.'''<br />


==Overview==
==DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.==
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.
<StructureSection load='1ds5' size='340' side='right'caption='[[1ds5]], [[Resolution|resolution]] 3.16&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==About this Structure==
==See Also==
1DS5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with MG and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DS5 OCA].
*[[Casein kinase 3D structures|Casein kinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10931203 10931203]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Zea mays]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:35:16 2007''

Latest revision as of 09:58, 7 February 2024

DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.

Structural highlights

1ds5 is a 8 chain structure with sequence from Homo sapiens and Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.16Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ds5, resolution 3.16Å

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