Structure of the catalytic domain of Mre11 from Chaetomium thermophilum

Acta Crystallographica Section F: Structural Biology Communications

Volumn 71, Issue , 2015, Pages 752-757

  Seifert, Florian Ulrich ^a   Lammens, Katja ^a   Hopfner, Karl Peter ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

Mre11 nuclease; MRN complex

Indexed keywords

CHAETOMIUM THERMOPHILUM; EUKARYOTA;

DNA; DNA LIGASE; FUNGAL PROTEIN; RECOMBINANT PROTEIN;

CHAETOMIUM; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; DNA REPAIR; DOUBLE STRANDED DNA BREAK; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN MOTIF; PROTEIN MULTIMERIZATION; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID MOTIFS; CHAETOMIUM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DNA; DNA BREAKS, DOUBLE-STRANDED; DNA REPAIR; DNA REPAIR ENZYMES; ESCHERICHIA COLI; FUNGAL PROTEINS; GENE EXPRESSION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 84931069419     PISSN: None     EISSN: 2053230X     Source Type: Journal    
DOI: 10.1107/S2053230X15007566     Document Type: Article

References (40)

1. Adams, P. D. et al. (2010). Acta Cryst. D66, 213-221.
2. Aguilera, A. & Gómez-González, B. (2008). Nature Rev. Genet. 9, 204-217.
3. Arthur, L. M., Gustausson, K., Hopfner, K.-P., Carson, C. T., Stracker, T. H., Karcher, A., Felton, D., Weitzman, M. D., Tainer, J. & Carney, J. P. (2004). Nucleic Acids Res. 32, 1886-1893.
4. Cadet, J., Ravanat, J. L., TavernaPorro, M., Menoni, H. & Angelov, D. (2012). Cancer Lett. 327, 5-15.
5. Chapman, J. R., Taylor, M. R. G. & Boulton, S. J. (2012). Mol. Cell, 47, 497-510.
6. Chiruvella, K. K., Liang, Z. & Wilson, T. E. (2013). Cold Spring Harb. Perspect. Biol. 5, a012757.
7. Costanzo, V., Robertson, K., Bibikova, M., Kim, E., Grieco, D., Gottesman, M., Carroll, D. & Gautier, J. (2001). Mol. Cell, 8, 137-147.
8. Das, D. et al. (2010). J. Mol. Biol. 397, 647-663.
9. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
10. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
11. Evans, P. (2006). Acta Cryst. D62, 72-82.
12. Evans, P. R. (2011). Acta Cryst. D67, 282-292.
13. Gapud, E. J. & Sleckman, B. P. (2011). Cell Cycle, 10, 1928-1935.
14. Goujon, M., McWilliam, H., Li, W., Valentin, F., Squizzato, S., Paern, J. & Lopez, R. (2010). Nucleic Acids Res. 38, W695-W699.
15. Hanahan, D. & Weinberg, R. A. (2011). Cell, 144, 646-674.
16. Hopfner, K. P., Karcher, A., Craig, L., Woo, T. T., Carney, J. P. & Tainer, J. A. (2001). Cell, 105, 473-485.
17. Kabsch, W. (2010a). Acta Cryst. D66, 125-132.
18. Kabsch, W. (2010b). Acta Cryst. D66, 133-144.
19. Krissinel, E. & Henrick, K. (2007). J. Mol. Biol. 372, 774-797.
20. Lam, I. & Keeney, S. (2014). Cold Spring Harb. Perspect. Biol. 7, a016634.
21. Lammens, K., Bemeleit, D. J., Möckel, C., Clausing, E., Schele, A., Hartung, S., Schiller, C. B., Lucas, M., Angermüller, C., Söding, J., Strässer, K. & Hopfner, K. P. (2011). Cell, 145, 54-66.
22. Lim, H. S., Kim, J. S., Park, Y. B., Gwon, G. H. & Cho, Y. (2011). Genes Dev. 25, 1091-1104.
23. Limbo, O., Moiani, D., Kertokalio, A., Wyman, C., Tainer, J. A. & Russell, P. (2012). Nucleic Acids Res. 40, 11435-11449.
24. Lisby, M., Barlow, J. H., Burgess, R. C. & Rothstein, R. (2004). Cell, 118, 699-713.
25. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C. & Read, R. J. (2007). J. Appl. Cryst. 40, 658-674.
26. Mehta, A. & Haber, J. E. (2014). Cold Spring Harb. Perspect. Biol. 6, a016428.
27. Möckel, C., Lammens, K., Schele, A. & Hopfner, K.-P. (2012). Nucleic Acids Res. 40, 914-927.
28. Myung, K., Chen, C. & Kolodner, R. D. (2001). Nature (London), 411, 1073-1076.
29. Myung, K., Datta, A. & Kolodner, R. D. (2001). Cell, 104, 397-408.
30. Park, Y. B., Chae, J., Kim, Y. C. & Cho, Y. (2011). Structure, 19, 1591-1602.
31. Schiller, C. B., Lammens, K., Guerini, I., Coordes, B., Feldmann, H., Schlauderer, F., Möckel, C., Schele, A., Strässer, K., Jackson, S. P. & Hopfner, K.-P. (2012). Nature Struct. Mol. Biol. 19, 693-700.
32. Schiller, C. B., Seifert, F. U., Linke-Winnebeck, C. & Hopfner, K.-P. (2014). Cold Spring Harb. Perspect. Biol. 6, a017962.
33. Shibata, A. et al. (2014). Mol. Cell, 53, 7-18.
34. Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Söding, J., Thompson, J. D. & Higgins, D. G. (2011). Mol. Syst. Biol. 7, 539.
35. Sutherland, B. M., Bennett, P. V., Sidorkina, O. & Laval, J. (2000). Proc. Natl Acad. Sci. USA, 97, 103-108.
36. Trujillo, K. M., Yuan, S.-S. F., Lee, E.-Y. P. & Sung, P. (1998). J. Biol. Chem. 273, 21447-21450.
37. Truong, L. N., Li, Y., Shi, L. Z., Hwang, P. Y.-H., He, J., Wang, H., Razavian, N., Berns, M. W. & Wu, X. (2013). Proc. Natl Acad. Sci. USA, 110, 7720-7725.
38. Williams, R. S., Moncalian, G., Williams, J. S., Yamada, Y., Limbo, O., Shin, D. S., Groocock, L. M., Cahill, D., Hitomi, C., Guenther, G., Moiani, D., Carney, J. P., Russell, P. & Tainer, J. A. (2008). Cell, 135, 97-109.
39. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
40. Xu, Z., Zan, H., Pone, E. J., Mai, T. & Casali, P. (2012). Nature Rev. Immunol. 12, 517-531.