1puc

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1puc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1puc OCA], [http://www.ebi.ac.uk/pdbsum/1puc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1puc RCSB]</span>
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[[Category: Khazanovich, N.]]
[[Category: Khazanovich, N.]]
[[Category: Michalak, M.]]
[[Category: Michalak, M.]]
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[[Category: CPS]]
 
[[Category: cell cycle]]
[[Category: cell cycle]]
[[Category: domain swapping]]
[[Category: domain swapping]]
[[Category: strand-exchanged dimer]]
[[Category: strand-exchanged dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:29:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:04:40 2008''

Revision as of 20:04, 30 March 2008


PDB ID 1puc

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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