1puc
From Proteopedia
(New page: 200px<br /><applet load="1puc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1puc, resolution 1.95Å" /> '''P13SUC1 IN A STRAND-...) |
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| - | [[Image:1puc.gif|left|200px]]<br /><applet load="1puc" size=" | + | [[Image:1puc.gif|left|200px]]<br /><applet load="1puc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1puc, resolution 1.95Å" /> | caption="1puc, resolution 1.95Å" /> | ||
'''P13SUC1 IN A STRAND-EXCHANGED DIMER'''<br /> | '''P13SUC1 IN A STRAND-EXCHANGED DIMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND. p13(suc1) from fission yeast is a member of the CDC28 kinase | + | BACKGROUND. p13(suc1) from fission yeast is a member of the CDC28 kinase specific (CKS) class of cell-cycle control proteins, that includes CKS1 from budding yeast and the human homologues CksHs1 and CksHs2. p13(suc1) participates in the regulation of p34(cdc2), a cyclin-dependent kinase controlling the G1-S and the G2-M transitions of the cell cycle. The CKS proteins are believed to exert their regulatory activity by binding to the kinase, in which case their function may be governed by their conformation or oligomerization state. Previously determined X-ray structures of p13(suc1), CksHs1 and CksHs2 show that these proteins share a common fold but adopt different oligomeric states. Monomeric forms of p13(suc1) and CksHs1 have been solved. In addition, CksHs2 and p13(suc1) have been observed by X-ray crystallography in assemblies of strand-exchanged dimers. Analysis of various assemblies of the CKS proteins, as found in different crystal forms, should help to clarify their role in cell-cycle control. RESULTS. We report the X-ray crystal structure of p13(suc1) to 1.95 A resolution in space group C2221. It is present in the crystals as a strand-exchanged dimer. The overall monomeric fold is preserved in each lobe of the dimer but a single beta-strand (Ile94-Asp102) is exchanged between the central beta-sheets of each molecule. CONCLUSIONS. Strand exchange, which has been observed for p13(suc1) in two different space groups, and for CksHs2, is now confirmed to be an intrinsic feature of the CKS family. A switch between levels of assembly may serve to coordinate the function of the CKS proteins in cell-cycle control. |
==About this Structure== | ==About this Structure== | ||
| - | 1PUC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with CPS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PUC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with <scene name='pdbligand=CPS:'>CPS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Schizosaccharomyces pombe]] | [[Category: Schizosaccharomyces pombe]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bateman, K | + | [[Category: Bateman, K S.]] |
[[Category: Chernaia, M.]] | [[Category: Chernaia, M.]] | ||
| - | [[Category: James, M | + | [[Category: James, M N.G.]] |
[[Category: Khazanovich, N.]] | [[Category: Khazanovich, N.]] | ||
[[Category: Michalak, M.]] | [[Category: Michalak, M.]] | ||
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[[Category: strand-exchanged dimer]] | [[Category: strand-exchanged dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:42 2008'' |
Revision as of 12:32, 21 February 2008
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P13SUC1 IN A STRAND-EXCHANGED DIMER
Overview
BACKGROUND. p13(suc1) from fission yeast is a member of the CDC28 kinase specific (CKS) class of cell-cycle control proteins, that includes CKS1 from budding yeast and the human homologues CksHs1 and CksHs2. p13(suc1) participates in the regulation of p34(cdc2), a cyclin-dependent kinase controlling the G1-S and the G2-M transitions of the cell cycle. The CKS proteins are believed to exert their regulatory activity by binding to the kinase, in which case their function may be governed by their conformation or oligomerization state. Previously determined X-ray structures of p13(suc1), CksHs1 and CksHs2 show that these proteins share a common fold but adopt different oligomeric states. Monomeric forms of p13(suc1) and CksHs1 have been solved. In addition, CksHs2 and p13(suc1) have been observed by X-ray crystallography in assemblies of strand-exchanged dimers. Analysis of various assemblies of the CKS proteins, as found in different crystal forms, should help to clarify their role in cell-cycle control. RESULTS. We report the X-ray crystal structure of p13(suc1) to 1.95 A resolution in space group C2221. It is present in the crystals as a strand-exchanged dimer. The overall monomeric fold is preserved in each lobe of the dimer but a single beta-strand (Ile94-Asp102) is exchanged between the central beta-sheets of each molecule. CONCLUSIONS. Strand exchange, which has been observed for p13(suc1) in two different space groups, and for CksHs2, is now confirmed to be an intrinsic feature of the CKS family. A switch between levels of assembly may serve to coordinate the function of the CKS proteins in cell-cycle control.
About this Structure
1PUC is a Single protein structure of sequence from Schizosaccharomyces pombe with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the yeast cell-cycle control protein, p13suc1, in a strand-exchanged dimer., Khazanovich N, Bateman K, Chernaia M, Michalak M, James M, Structure. 1996 Mar 15;4(3):299-309. PMID:8805536
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