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1qb3

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{{STRUCTURE_1qb3| PDB=1qb3 | SCENE= }}
{{STRUCTURE_1qb3| PDB=1qb3 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1'''
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===CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Cell cycle mutagenesis domain swapping]]
[[Category: Cell cycle mutagenesis domain swapping]]
[[Category: Cyclin-dependent kinase]]
[[Category: Cyclin-dependent kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:31:54 2008''

Revision as of 14:31, 27 July 2008

Image:1qb3.png

Template:STRUCTURE 1qb3

CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1

Template:ABSTRACT PUBMED 10997903

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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