1ds5: Difference between revisions

Revision as of 13:19, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1DS5 is a Protein complex structure of sequences from Zea mays with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

ReferenceReference

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:10931203

Page seeded by OCA on Thu Feb 21 12:19:56 2008

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OCA

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-[[Image:1ds5.gif|left|200px]]<br />
+[[Image:1ds5.gif|left|200px]]<br /><applet load="1ds5" size="350" color="white" frame="true" align="right" spinBox="true"
-<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==
-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.
+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.
 ==About this Structure==
-DS5 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].
+DS5 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 <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=AMP:'>AMP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS5 OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Battistutta, R.]]
 [[Category: Marin, O.]]
-[[Category: Moliner, E.De.]]
+[[Category: Moliner, E De.]]
-[[Category: Pinna, L.A.]]
+[[Category: Pinna, L A.]]
 [[Category: Sarno, S.]]
 [[Category: Zanotti, G.]]
@@ Line 26: / Line 25: @@
 [[Category: tetramer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:35:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:56 2008''