1jam

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1jam" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jam, resolution 2.18&Aring;" /> '''Crystal structure of...)
Current revision (07:38, 7 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1jam.gif|left|200px]]<br /><applet load="1jam" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1jam, resolution 2.18&Aring;" />
 
-
'''Crystal structure of apo-form of Z. Mays CK2 protein kinase alpha subunit'''<br />
 
-
==Overview==
+
==Crystal structure of apo-form of Z. Mays CK2 protein kinase alpha subunit==
-
Two novel crystal structures of Zea mays protein kinase CK2alpha catalytic, subunit, one in complex with the specific inhibitor, 4,5,6,7-tetrabromobenzotriazole (TBB) and another in the apo-form, were, solved at 2.2 A resolution. These structures were compared with those of, the enzyme in presence of ATP and GTP (the natural cosubstrates) and the, inhibitor emodin. Interaction of TBB with the active site of CK2alpha is, mainly due to van der Waals contacts, with the ligand fitting almost, perfectly the cavity. One nitrogen of the five-membered ring interacts, with two charged residues, Glu 81 and Lys 68, in the depth of the cavity, through two water molecules. These are buried in the active site and are, also generally found in the structures of CK2alpha enzyme analyzed so far, with the exception of the complex with emodin. In the N-terminal lobe, the, position of helix alphaC is particularly well preserved in all the, structures examined; the Gly-rich loop is displaced from the intermediate, position it has in the apo-form and in the presence of the natural, cosubstrates (ATP/GTP) to either an upper (with TBB) or a lower position, (with emodin). The selectivity of TBB for CK2 appears to be mainly, dictated by the reduced size of the active site which in most other, protein kinases is too large for making stable interactions with this, inhibitor.
+
<StructureSection load='1jam' size='340' side='right'caption='[[1jam]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1jam]] 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=1JAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JAM 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]] 2.18&#8491;</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=1jam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jam OCA], [https://pdbe.org/1jam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jam RCSB], [https://www.ebi.ac.uk/pdbsum/1jam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jam 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/ja/1jam_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=1jam ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1JAM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. 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=1JAM OCA].
+
*[[Casein kinase 3D structures|Casein kinase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole., Battistutta R, De Moliner E, Sarno S, Zanotti G, Pinna LA, Protein Sci. 2001 Nov;10(11):2200-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11604527 11604527]
+
[[Category: Large Structures]]
-
[[Category: Non-specific serine/threonine protein kinase]]
+
-
[[Category: Single protein]]
+
[[Category: Zea mays]]
[[Category: Zea mays]]
-
[[Category: Battistutta, R.]]
+
[[Category: Battistutta R]]
-
[[Category: Moliner, E.De.]]
+
[[Category: De Moliner E]]
-
[[Category: Pinna, L.A.]]
+
[[Category: Pinna LA]]
-
[[Category: Sarno, S.]]
+
[[Category: Sarno S]]
-
[[Category: Zanotti, G.]]
+
[[Category: Zanotti G]]
-
[[Category: protein kinase fold]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:03:21 2007''
+

Current revision

Crystal structure of apo-form of Z. Mays CK2 protein kinase alpha subunit

PDB ID 1jam

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jam"
Personal tools