Proline-dependent oligomerization with arm exchange

Structure

Volumn 5, Issue 3, 1997, Pages 391-401

  Bergdoll, Marc ^a   Remy, Marie Hélène ^b   Cagnon, Christine ^c   Masson, Jean Michel ^b,c   Dumas, Philippe ^d  

^a INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^b INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE   (France)

^c INSA   (France)

^d INST DE BIOL MOLEC ET CELLULAIRE   (France)

Author keywords

arm exchange; folding; oligomerization; prolines

Indexed keywords

EID: 0031569328     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00196-2     Document Type: Article

References (52)

1. Goodsell, D.S. & Olson, A.J. (1993). Soluble proteins: size, shape and function. TIBS 18, 65-68.
2. Richardson, J.S. (1981). The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-339.
3. 4 apo-lactate dehydrogenase. J. Mol. Biol. 198, 445-467.
4. Bennett, M.J., Choe, S. & Eisenberg, D. (1994). Refined structure of dimeric diphtheria toxin at 2.0Å resolution. Prot. Sci. 3, 1444-1463.
5. Bennett, M.J., Schlunegger, M.P. & Eisenberg, D. (1995). 3D domain swapping: a mechanism for oligomer assembly. Prot. Sci. 4, 2455-2468.
6. Liddington, R.C., Yan, Y., Moulai, J., Sahli, R., Benjamin, T.L. & Harrison, S. (1991). Structure of simian virus 40 at 3.8 Å resolution. Nature 354, 278-284.
7. Dumas, P., Bergdoll, M., Cagnon, C. & Masson, J.M. (1994). Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering. EMBO J. 13, 2483-2492.
8. Gatignol, A., Durand, H. & Tiraby, G. (1988). Bleomycin resistance conferred by drug binding protein. FEBS Lett. 230, 171-175.
9. Rydel, T.J., Tulinski, A., Bode, W. & Huber, R. (1991). The refined structure of the Hirudin-Thrombin Complex. J. Mol. Biol. 221, 583-601.
10. Chen, L. & Hol, W.G.J. (1992). Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Biochem. 31, 4959-4964.
11. Cedergren-Zeppezauer, E.S., Larsson, G., Nyman, P.O., Dauter, Z. & Wilson, K.S. (1992). Crystal structure of dUTPase. Nature 355, 740-743.
12. Eck, M. & Sprang, S. (1989). The structure of Tumor Necrosis Factor-α at 2.0 Å resolution. J. Biol. Chem. 264, 17595-17605.
13. Fita, I., Silva, A.M., Murthy, M.R.N. & Rossmann, M.G. (1986). The refined structure of beef liver catalase at 2.5A resolution. Acta Cryst. B 42, 497-501.
14. Remington, S., Wiegand, G. & Huber, R. (1982). Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution. J. Mol. Biol. 158, 111-152.
15. Russel, R.J.M., Hough, D.W., Danson, M.J. & Taylor, G.L. (1994). The crystal structure of citrate synthase from the thermophilic Archaeon, Themoplasma acidophilum. Structure 2, 1157-1167.
16. Wodlawer, A., Bott, R. & Sjolin, L. (1982). The refined crystal structure of ribonuclease A at 2.0 Å resolution. J. Biol. Chem. 257, 1325-1332.
17. Mazzarella, L., Capasso, S., Demasi, D., DiLorenzo, G., Mattia, C.A. & Zagari, A. (1993). Bovine seminal ribonuclease: structure at 1.9 Å resolution. Acta Cryst. D 49, 389-402.
18. Piccoli, R., Tamburrini, M., Picciali, G., DiDonato, A., Parente, A. & d'Alessio, G. (1 992). The dual-mode quaternary structure of seminal RNase. Proc. Natl. Acad. Sci. USA 89, 1870-1874.
19. DiDonato, A., Cafaro, V. & d'Alessio, G. (1994). Ribonuclease A can be transformed into a dimeric ribonuclease with antitumor activity. J. Biol. Chem. 269, 17394-17396.
20. Mol, C.D., Harris, J.M., McIntosh, E.M. & Tainer, J.A. (1996). Human dUTP pyrophosphatase: uracil recognition by a β hairpin and active sites formed by three separate subunits. Structure 4, 1077-1092.
21. McGeoch, D.J. (1990). Protein sequence comparisons show that the 'pseudoproteases' encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family. Nucl. Acids Res. 18, 4105-4110.
22. Climie, S., Lutz, T., Radul, J., Sumner-Smith, M., Vandenberg, E. & McIntosh, E. (1994). Expression of trimeric human dUTP pyrophosphatase in Escherichia coli and purification of the enzyme. Protein Expr. Purif. 5, 252-258.
23. Brandts, J.F., Halvorson, H.R. & Brennan, M. (1975). Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochem. 14, 4953-4963.
24. Tonelli, A.E. (1974). Conformational characteristics of polypeptides containing isolated L-proline residues with cis peptide bonds. J. Mol. Biol. 86, 627-635.
25. Szyperski, T., Guntert, P., Stone, S.R. & Wuthrich, K. (1992). Nuclear magnetic resonance solution structure of hirudin (1-51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain. J. Mol. Biol. 228, 1193-1205.
26. Bourne, Y., et al., & Tainer, J.A. (1995). Crystal structure of the cell cycle-regulatory protein sud reveals a β hinge conformation switch. Proc. Natl. Acad. Sci. USA 92, 10232-10236.
27. cdc2-interacting cell cycle control protein. EMBO J. 14, 1004-1014.
28. cksphy. Biochem. 35, 5577-5585.
29. Hohenester, E. & Jansonius, J.N. (1994). Crystalline mitochondrial aspartate aminotransferase exists in only two conformations. J. Mol. Biol. 236, 963-968.
30. Bennett, M.J. & Eisenberg, D. (1994). Refined structure of monomeric diphtheria toxin at 2.3A resolution. Prot. Sci. 3, 464-1475.
31. +-ATPase oligomerisation. Am. J. Physiol. C265, C1169-C1174.
32. Mazzarella, K., Vitagliano, L. & Zagari, A. (1995). Swapping structural determinants of ribonucleases: an energetic analysis of the hinge peptide 16-22. Proc. Natl. Acad. Sci. USA 92, 3799-3803.
33. Bartos, E. & Uziel, M. (1961). Guinea pig pancreas ribonucleases. Separation by ion exchange chromatography and the subcellular distribution of these enzymes. J. Biol. Chem. 236, 1697-1700.
34. Hopper, P., Harrison, S.C. & Sauer, R.T. (1984). Structure of tomato bushy stunt virus V. Coat protein sequence determination and its structural implications. J. Mol. Biol. 177, 701-713.
35. Speir, J.A., Munshi, S., Wang, G., Baker, T.S. & Johnson, J.E. (1994). Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structured, 63-78.
36. Valegard, K., Murray, J.B., Stockley, P.G., Stonehouse, N.J. & Liljas, L. (1994). Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371, 623-626.
37. Stonehouse, N.J., Valegard, K., Golmohammadi, R., van den Worm, S., Stockley, P.G. & Liljas, L. (1996). Crystal structures of MS2 capsids with mutations in the subunit FG loop. J. Mol. Biol. 256, 330-339.
38. UWGCG (1994). Program Manual for the Wisconsin Package.
39. Bernstein, F.C. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
40. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
41. Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219-220.
42. Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D, version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
43. Cagnon, C., Valverde, V. & Masson, J.-M. (1991). A new family of sugar-inducible expression vectors for Escherichia coli. Protein Eng. 4, 843-847.
44. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
45. Vainshtein, B.K., et al., & Rossmann, M.G. (1986). Three-dimensional structure of catalase from Penicillium vitale at 2.0 Å resolution. J. Mol. Biol. 188, 49-61.
46. Gouet, P., Jouve, H.-M. & Dideberg, O. (1995). Crystal structure of Proteus mirabilis catalase with and without bound NADPH. J. Mol. Biol. 249, 933-954.
47. Murshudov, G.N., et al., & Wilson, K.S. (1995). Three-dimensional structure of catalase from Micococcus lysodeikticus at 1.5 Å resolution. FEBS Lett. 312, 127-131.
48. Bravo, J., et al., & Fita, I. (1995). Crystal structure of catalase HPII from Escherichia coli. Structure 3, 491-502.
49. Jäger, J., Moser, M., Sauder, U. & Jansonius, J.N. (1994). Crystal structure of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms. J. Mol. Biol. 239, 285-305.
50. Malashkevitch, V.N., Strokopytov, B.V., Borisov, V.V., Dauter, Z., Wilson, K.S. & Torchinsky, Y.M. (1995). Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 Å resolution. J. Mol. Biol. 247, 111-124.
51. Hogle, J.M., Maeda, A. & Harrison, S.C. (1986). Structure and assembly of turnip crinkle virus I. X-ray crystallographic structure analysis at 3.2 Å resolution. J. Mol. Biol. 191, 625-638.
52. Sorger, P.K., Stockley, P.G. & Harrison, S.C. (1986). Structure and assembly of turnip crinkle virus II. Mechanism of reassembly in vitro. J. Mol. Biol. 191, 639-658.