1qb3
From Proteopedia
(New page: 200px<br /><applet load="1qb3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qb3, resolution 3.Å" /> '''CRYSTAL STRUCTURE OF T...) |
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| - | [[Image:1qb3.jpg|left|200px]]<br /><applet load="1qb3" size=" | + | [[Image:1qb3.jpg|left|200px]]<br /><applet load="1qb3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qb3, resolution 3.Å" /> | caption="1qb3, resolution 3.Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1'''<br /> | '''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The Saccharomyces cerevisiae protein Cks1 (cyclin-dependent | + | BACKGROUND: The Saccharomyces cerevisiae protein Cks1 (cyclin-dependent kinase subunit 1) is essential for cell-cycle progression. The biological function of Cks1 can be modulated by a switch between two distinct molecular assemblies: the single domain fold, which results from the closing of a beta-hinge motif, and the intersubunit beta-strand interchanged dimer, which arises from the opening of the beta-hinge motif. The crystal structure of a cyclin-dependent kinase (Cdk) in complex with the human Cks homolog CksHs1 single-domain fold revealed the importance of conserved hydrophobic residues and charged residues within the beta-hinge motif. RESULTS: The 3.0 A resolution Cks1 structure reveals the strict structural conservation of the Cks alpha/beta-core fold and the beta-hinge motif. The beta hinge identified in the Cks1 structure includes a novel pivot and exposes a cluster of conserved tyrosine residues that are involved in Cdk binding but are sequestered in the beta-interchanged Cks homolog suc1 dimer structure. This Cks1 structure confirms the conservation of the Cks anion-binding site, which interacts with sidechain residues from the C-terminal alpha helix of another subunit in the crystal. CONCLUSIONS: The Cks1 structure exemplifies the conservation of the beta-interchanged dimer and the anion-binding site in evolutionarily distant yeast and human Cks homologs. Mutational analyses including in vivo rescue of CKS1 disruption support the dual functional roles of the beta-hinge residue Glu94, which participates in Cdk binding, and of the anion-binding pocket that is located 22 A away and on an opposite face to Glu94. The Cks1 structure suggests a biological role for the beta-interchanged dimer and the anion-binding site in targeting Cdks to specific phosphoproteins during cell-cycle progression. |
==About this Structure== | ==About this Structure== | ||
| - | 1QB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1QB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QB3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arvai, A | + | [[Category: Arvai, A S.]] |
| - | [[Category: Bernstein, S | + | [[Category: Bernstein, S L.]] |
[[Category: Bourne, Y.]] | [[Category: Bourne, Y.]] | ||
| - | [[Category: Reed, S | + | [[Category: Reed, S I.]] |
| - | [[Category: Tainer, J | + | [[Category: Tainer, J A.]] |
| - | [[Category: Watson, M | + | [[Category: Watson, M H.]] |
[[Category: cell cycle mutagenesis domain swapping]] | [[Category: cell cycle mutagenesis domain swapping]] | ||
[[Category: cyclin-dependent kinase]] | [[Category: cyclin-dependent kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:46 2008'' |
Revision as of 12:37, 21 February 2008
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CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1
Overview
BACKGROUND: The Saccharomyces cerevisiae protein Cks1 (cyclin-dependent kinase subunit 1) is essential for cell-cycle progression. The biological function of Cks1 can be modulated by a switch between two distinct molecular assemblies: the single domain fold, which results from the closing of a beta-hinge motif, and the intersubunit beta-strand interchanged dimer, which arises from the opening of the beta-hinge motif. The crystal structure of a cyclin-dependent kinase (Cdk) in complex with the human Cks homolog CksHs1 single-domain fold revealed the importance of conserved hydrophobic residues and charged residues within the beta-hinge motif. RESULTS: The 3.0 A resolution Cks1 structure reveals the strict structural conservation of the Cks alpha/beta-core fold and the beta-hinge motif. The beta hinge identified in the Cks1 structure includes a novel pivot and exposes a cluster of conserved tyrosine residues that are involved in Cdk binding but are sequestered in the beta-interchanged Cks homolog suc1 dimer structure. This Cks1 structure confirms the conservation of the Cks anion-binding site, which interacts with sidechain residues from the C-terminal alpha helix of another subunit in the crystal. CONCLUSIONS: The Cks1 structure exemplifies the conservation of the beta-interchanged dimer and the anion-binding site in evolutionarily distant yeast and human Cks homologs. Mutational analyses including in vivo rescue of CKS1 disruption support the dual functional roles of the beta-hinge residue Glu94, which participates in Cdk binding, and of the anion-binding pocket that is located 22 A away and on an opposite face to Glu94. The Cks1 structure suggests a biological role for the beta-interchanged dimer and the anion-binding site in targeting Cdks to specific phosphoproteins during cell-cycle progression.
About this Structure
1QB3 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions., Bourne Y, Watson MH, Arvai AS, Bernstein SL, Reed SI, Tainer JA, Structure. 2000 Aug 15;8(8):841-50. PMID:10997903
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