1qb3
From Proteopedia
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| - | [[Image:1qb3.jpg|left|200px]] | + | [[Image:1qb3.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1''' | + | {{Structure |
| + | |PDB= 1qb3 |SIZE=350|CAPTION= <scene name='initialview01'>1qb3</scene>, resolution 3.Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QB3 is a [ | + | 1QB3 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10997903 10997903] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cyclin-dependent kinase]] | [[Category: cyclin-dependent kinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:35:22 2008'' |
Revision as of 11:35, 20 March 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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