2.5 Å resolution crystal structure of the motile major sperm protein (MSP) of Ascaris suum

Journal of Molecular Biology

Volumn 263, Issue 2, 1996, Pages 284-296

  Bullock, Timothy L ^a   Roberts, Thomas M ^b   Stewart, Murray ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b FLORIDA STATE UNIVERSITY   (United States)

Author keywords

Ascaris; Cell motility; Crystal structure; Immunoglobulin fold; Major sperm protein

Indexed keywords

POLYPEPTIDE; PROTEIN; HELMINTH PROTEIN; MAJOR SPERM PROTEIN, NEMATODE;

ARTICLE; ASCARIS SUUM; BETA CHAIN; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; SPERMATOZOON MOTILITY; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; ANIMAL; CELL MOTION; CHEMISTRY; MALE; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

ASCARIS; ASCARIS SUUM; BACTERIA (MICROORGANISMS);

AMINO ACID SEQUENCE; ANIMALS; ASCARIS SUUM; CELL MOVEMENT; CRYSTALLOGRAPHY, X-RAY; HELMINTH PROTEINS; MALE; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

EID: 0030601552     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0575     Document Type: Article

References (44)

1. 1 ATPase, Acta Crystallog. sect. D, 52, 30-42.
2. Alberts, B., Bray, D., Lewis, J., Raff, M., Roberts, K. & Watson, J. D. (1994). Molecular Biology of the Cell. 3rd edit., Garland Press, New York.
3. Auffray, C., Behar, G., Bois, F., Boucher, C. da Silva, C., Devignes, M. D., Duprat, S., Houlgatte, R., Jumeau, M. M., Lamy, B., Lorenzo, F., Mitchell, H., Mariage-Samson, R., Pietu, G., Pouliot, Y., Sebastiani-Kabatchis, C. & Tessier, A. (1995). IMAGE: integrated molecular analysis of the human genome and its expression. C. R. H. Acad. Sci., III, Sci. Vie, 318, 263-272.
4. Bork, P., Holm, L. & Sander, C. (1994). The immunoglobulin fold. Structural classification, sequence patterns and a common core. J. Mol. Biol. 242, 309-320.
5. Brünger, A. T. (1992). Free R value: a novel statistical quality for assessing the accuracy of crystal structures. Nature, 355, 472-474.
6. Bullock, T. L., Parthasarathy, G., King, K. L., Kent, H. M., Roberts, T. M. & Stewart, M. (1996). New crystal forms of the motile major sperm protein (MSP) of Ascaris suum. J. Struct. Biol. 116, 432-437.
7. Bullit, E. & Makowski, L. (1995). Structural polymorphism of bacterial adhesion pili. Nature, 373, 164-167.
8. Collaborative Computational Project, number 4 (1994). The CCP4 suite: programmes for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
9. Condeelis, J. (1993). Life at the leading edge: the formation of cell protrusions. Annu. Rev. Cell Biol. 9, 411-444.
10. Haaf, A., Butler, P. J. G., Kent, H. M., Fearnley, I. M., Roberts, T. M., Neuhaus, D. & Stewart, M. (1996). The motile major sperm protein (MSP) from Ascaris suum is a symmetric dimer in solution. J. Mol. Biol. 260, 251-260.
11. Harpaz, Y. & Chothia, C. (1994). Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238, 528-539.
12. Heath, J. Horfield, B. F. (1991). Cell locomotion: new research tests old ideas on membrane and cytoskeletal flow. Cell Motil. Cytoskel. 18, 245-257.
13. Holmgren, A. & Branden, C.-I. (1989). Crystal structure of chaperonin protein PapD reveals an immunoglobin fold. Nature, 342, 248-251.
14. Holmgren, A., Kuehn, M. J., Branden, C.-I. & Hultgren, S. J. (1992). Conserved immunoglobulin-like features in a family of periplasmic pilus chaperonins in bacteria. EMBO J. 11, 1617-1622.
15. Italiano, J. E., Roberts, T. M., Stewart, M. & Fontana, C. (1996). Reconstitution in vitro of the motile apparatus from the amoeboid sperm of Ascaris: direct evidence that filament assembly and bundling move membranes. Cell, 84, 105-114.
16. Janin, J. & Chothia, C. (1991). The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030.
17. Jones, S. & Thornton, J. M. (1996). Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA, 93, 13-20.
18. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and for locating errors in these models. Acta Crystallog. sect. A, 47, 110-119.
19. King, K. L., Stewart, M., Roberts, T. M. & Seavy, M. (1992). Structure and macromolecular assembly of two isoforms of the major sperm protein (MSP) from the amoeboid sperm of the nematode, Ascaris suum. J. Cell Sci. 101, 847-857.
20. King, K. L., Stewart, M. & Roberts, T. M. (1994). Supramolecular assemblies of the Ascaris suum major sperm protein (MSP) associated with amoeboid cell motility. J. Cell Sci. 107, 2941-2949.
21. Klug, A., Crick, F. H. C. & Wyckoff, H. W. (1955). Diffraction by helical structures. Acta Crystallog. 11, 199-213.
22. Kraulis, P. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
23. Kuehn, M. J., Ogg, D. J., Kihlberg, J., Slonim, L. N., Flemmer, K., Bergfors, T., & Hultgren, S. J. (1993). Structural basis of pilus subunit recognition by the PapD chaperone. Science, 262, 1234-1241.
24. 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. Crystallog. 26, 283-291.
25. Laemmli, U. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
26. Lee, J., Ishihara, A. & Jacobson, K. (1993). How do cells slide along surfaces? Trends Cell Biol. 3, 366-370.
27. Main, A. L., Harvey, T. S., Baron, M., Boyd, J. & Campbell, I. D. (1992). The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell, 71, 671-678.
28. McLachlan, A. D. & Stewart, M. (1975). Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98, 293-304.
29. Oliver, T., Lee, J. & Jacobson, K. (1994). Forces exerted by locomoting cells. Seminar Cell Biol. 5, 139-147.
30. Parge, H. E., Forest, K. T., Hickey, M. J., Christenson, D. A., Getzoff, E. D. & Tainer, J. A. (1995). Structure of the fibre-forming protein pilin at 2.6 Å resolution. Nature, 378, 32-38.
31. Roberts, T. M. & King, K. L. (1991). Centripetal flow and directed reassembly of the major sperm protein (MSP) cytoskeleton in the amoeboid sperm of the nematode, Ascaris suum. Cell Motil. Cytoskel. 20, 228-241.
32. Roberts, T. M. & Stewart, M. (1995). Nematode sperm locomotion. Curr. Opin. Cell Biol. 7, 13-17.
33. Ryu, S. E., Kwong, P. D., Truneh, A., Porter, T. G., Arthos, J., Rosenberg, M., Dai, X., Xuong, N. H., Axel, R., Sweet, R. W. & Hendrickson, W. A. (1990). Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature, 348, 419-426.
34. Sepsenwol, S., Ris, H. & Roberts, T. M. (1989). A unique cytoskeleton associated with crawling in amoeboid sperm of the nematode, Ascaris suum. J. Cell Biol. 108, 55-66.
35. Skehel, P. A., Martin, K. C., Kandel, E. R. & Bartsch, D. (1995). A VAMP-binding protein from Aplysia required for neurotransmitter release. Science, 269, 1580-1583.
36. Stewart, M., King, K. L. & Roberts, T. M. (1993). Crystallization of the motile major sperm protein (MSP) of the nematode Ascaris suum. J. Mol. Biol. 232, 298-300.
37. Stewart, M., King, K. L. & Roberts, T. M. (1994). The motile major sperm protein (MSP) of Ascaris suum forms filaments constructed from two helical subfilaments. J. Mol. Biol. 242, 60-71.
38. Stossel, T. P. (1993). On the crawling of animal cells. Science, 260, 1086-1094.
39. Studier, F. W., Rosenburg, A. H., Dunn, J. J. & Dubedorff, J. W. (1990). Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
40. Südhof, T. C. (1995). The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature, 375, 645-653.
41. Theriot, J. A. (1996). Worm sperm and advances in cell locomotion. Cell, 84, 1-4.
42. Theriot, J. A. & Mitchison, T. J. (1992). The nucleation-release model of actin filaments dynamics in cell motility. Trends Cell Biol. 2, 219-222.
43. Tronrud, D. E., TenEyck, L. F. & Mathews, B. W. (1987). An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A, 43, 489-503.
44. Williams, A. F. & Barclay, A. N. (1988). The immunoglobulin superfamily-domains for cell surface recognition. Annu. Rev. Immunol. 6, 381-405.