Crystal structure of the yeast cell-cycle control protein, p13suc1, in a strand-exchanged dimer

Structure

Volumn 4, Issue 3, 1996, Pages 299-309

  Khazanovich, N ^a   Bateman, K S ^a   Chernaia, M ^a   Michalak, M ^a   James, M N G ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Cell cycle; Domain swapping; p13suc1; Strand exchanged dimer; X ray structure

Indexed keywords

CARRIER PROTEIN; CELL CYCLE PROTEIN; CKS2 PROTEIN, HUMAN; FUNGAL PROTEIN; PROTEIN KINASE; SCHIZOSACCHAROMYCES POMBE PROTEIN; SUC1 PROTEIN, S POMBE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SCHIZOSACCHAROMYCES; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CARRIER PROTEINS; CELL CYCLE PROTEINS; CRYSTALLOGRAPHY, X-RAY; FUNGAL PROTEINS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS; SEQUENCE ALIGNMENT;

SCHIZOSACCHAROMYCES;

EID: 0030584661     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00034-2     Document Type: Article

References (39)

1. Hayles, J., Aves, S. & Nurse, P. (1986). suc1 is an essential gene involved in both the cell cycle and growth in fission yeast. EMBO J. 5, 3373-3379.
2. + encodes a predicted 13-kilodalton protein that is essential for cell viability and is directly involved in the division cycle of Schizosaccharomyces pombe. Mol. Cell. Biol. 7, 504-511.
3. cdc2 protein kinase during mitosis. Cell 58, 361-372.
4. Endicott, J.A. & Nurse, P. (1995). The cell cycle and suc1: from structure to function? Structure 3, 321-325.
5. cdc2 protein kinase. EMBO J. 6, 3507-3514.
6. Forsburg, S.L. & Nurse, P. (1991). Cell cycle regulation in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Annu. Rev. Cell Biol. 7, 227-256.
7. Nurse, P. & Bissett, Y. (1981). Gene required in G1 for commitment to cell cycle and in G2 for control of mitosis in fission yeast. Nature 292, 558-560.
8. Surana, U., Robitsch, H., Price, C., Schuster, T., Fitch, I. & Futcher, A.B. (1991). The role of CDC28 and cyclins during mitosis in the budding yeast S. cerevisiae. Cell 65, 145-161.
9. + of fission yeast encodes a protein kinase potentially regulated by phosphorylation. Cell 45, 261-268.
10. Dunphy, W.G. (1994). The decision to enter mitosis. Trends Cell. Biol. 4, 202-207.
11. Solomon, M.J. (1993). Activation of the various cyclin/cdc2 protein kinases. Curr. Opin. Cell Biol. 5, 180-186.
12. Hayles, J., Beach, D., Durkacz, B. & Nurse, P. (1986). The fission yeast cell cycle control gene cdc2; isolation of a sequence suc1, that suppresses cdc2 mutant function. Mol. Gen. Genet. 202, 291-293.
13. + gene, encodes a subunit of the cdc28 protein kinase complex. Mol. Cell. Biol. 9, 2034-2041.
14. suc1: implications for control of cell division cycle in plants. Protoplasma 161, 70-74.
15. suc1, examined in living cells. Proc. Natl. Acad. Sci. USA 91, 2176-2180.
16. Colas, P., Serras, F. & Van Loon, A.E. (1993). Microinjection of suc1 transcripts delays the cell cycle clock in Patella vulgata embryos. Int. J. Dev. Biol. 37, 589-94.
17. Dunphy, W.G. & Newport, J.W. (1989). Fission yeast p13 blocks mitotic activation and tyrosine dephosphorylation of the Xenopus cdc2 protein kinase. Cell 58, 181-191.
18. cdc2 kinase for intermediate filament proteins, in vitro. J. Biol. Chem. 267, 20937-20942.
19. cdc2-interacting cell cycle control protein. EMBO J. 14, 1004-1014.
20. Arvai, A.S., Bourne, Y., Hickey, M.J. & Tainer, J.A. (1995). Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain. J. Mol. Biol. 249, 835-842.
21. Parge, H.E., Arvai, A.S., Murtari, D.J., Reed, S.I. & Tainer, J.A. (1993). Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control. Science 262, 387-395.
22. Bourne, Y., et al., & Tainer, J.A. (1995). Crystal structure of the cell cycle-regulatory protein suc1 reveals a β-hinge conformational switch. Proc. Natl. Acad. Sci. USA 92, 10232-10236.
23. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
24. Bennett, M.J., Schlunegger, M.P. & Eisenberg, D. (1995). 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4, 2455-2468.
25. Mazzarella, L., et al., & Zagari, A. (1993). Bovine seminal ribonuclease: Structure at 1.9 Å resolution. Acta Cryst. D 49, 389-402.
26. Green, S.M., Gittis, A.G., Meeker, A.K. & Lattman, E.E. (1995). One-step evolution of a dimer from a monomeric protein. Nature Struct Biol. 2, 746-751.
27. Milburn, M.V., et al., & Wells, T.N.C. (1993). A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5. Nature 363, 172-176.
28. Lapatto, R., et al., & Slingsby C. (1991). High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin. J. Mol. Biol. 222, 1067-1083.
29. Bennett, M.J., Choe, S. & Eisenberg, D. (1994). Domain swapping: entangling alliances between proteins. Proc. Natl. Acad. Sci. USA 91, 3127-3131.
30. Carrell, R.W. & Evans, D.L.I. (1992). Serpins: mobile conformations in a family of proteinase inhibitors. Curr. Opin. Struct Biol. 2, 438-446.
31. Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
32. Brünger, A.T. (1993). X-PLOR: A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
33. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
34. Tronrud, D.E. (1992). Conjugate-direction minimization: an improved method for the refinement of macromolecules. Acta Cryst A 48, 912-916.
35. Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
36. Bernstein, F.C., et al., & Tasumi, M. (1977). The protein data bank: a computer based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
37. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
38. Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics 6, 219-220.
39. Nicholls, A., Sharp, K. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.