Structure of Escherichia coli RutC, a member of the YjgF family and putative aminoacrylate peracid reductase of the rut operon

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 11, 2012, Pages 1294-1299

  Knapik, Aleksandra Alicja ^a,b,c   Petkowski, Janusz Jurand ^a   Otwinowski, Zbyszek ^d   Cymborowski, Marcin Tadeusz ^a,b   Cooper, David Robert ^a,b   Chruszcz, Maksymilian ^a,b   Krajewska, Wanda Małgorzata ^c   Minor, Wladek ^a,b  

^a UNIVERSITY OF VIRGINIA   (United States)

^b New York Structural Genomics Research Consortium   (United States)

^c UNIVERSITY OF LODZ   (Poland)

^d UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

aminoacrylate; peroxy aminoacrylate; rut operon; RutC; YjgF superfamily

Indexed keywords

ESCHERICHIA COLI PROTEIN; OXIDOREDUCTASE; RUTC PROTEIN, E COLI;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; HYDROGEN BOND; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; OPERON; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE ANNOTATION; MOLECULAR SEQUENCE DATA; OPERON; OXIDOREDUCTASES; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN;

ESCHERICHIA COLI;

EID: 84869022149     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112041796     Document Type: Article

References (37)

1. Abagyan, R. & Totrov, M. (1997). Proteins, 29, Suppl. 1, 215-220.
2. Burman, J. D., Stevenson, C. E., Sawers, R. G. & Lawson, D. M. (2007). BMC Struct. Biol. 7, 30.
3. Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Cryst. D66, 12-21.
4. Cowtan, K. D. & Zhang, K. Y. J. (1999). Prog. Biophys. Mol. Biol. 72, 245-270.
5. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
6. Feng, J., Zhu, M., Schaub, M. C., Gehrig, P., Roschitzki, B., Lucchinetti, E. & Zaugg, M. (2008). Cardiovasc. Res. 80, 20-29.
7. Hall, T. A. (1999). Nucleic Acids Symp. Ser. 41, 95-98
8. Holm, L. & Rosenström, P. (2010). Nucleic Acids Res. 38, W545-W549.
9. Hutchinson, E. G. & Thornton, J. M. (1996). Protein Sci. 5, 212-220.
10. Kim, J.-M., Yoshikawa, H. & Shirahige, K. (2001). Genes Cells, 6, 507-517.
11. Kim, K.-S., Pelton, J. G., Inwood, W. B., Andersen, U., Kustu, S. & Wemmer, D. E. (2010). J. Bacteriol. 192, 4089-4102.
12. Knapik, A. A., Petkowski, J. J., Otwinowski, Z., Cymborowski, M. T., Cooper, D. R., Majorek, K. A., Chruszcz, M., Krajewska, W. M. & Minor, W. (2012). Proteins, 80, 2359-2368.
13. Lambrecht, J. A., Browne, B. A. & Downs, D. M. (2010). J. Biol. Chem. 285, 34401-34407.
14. Lambrecht, J. A., Flynn, J. M. & Downs, D.M. (2012). J. Biol. Chem. 287, 3454- 3461.
15. Manjasetty, B. A., Delbrück, H., Pham, D. T., Mueller, U., Fieber-Erdmann, M., Scheich, C., Sievert, V., Büssow, K., Niesen, F. H.,Weihofen,W., Loll, B., Saenger, W., Heinemann, U. & Neisen, F. H. (2004). Proteins, 54, 797-800.
16. Minor, W., Cymborowski, M., Otwinowski, Z. & Chruszcz, M. (2006). Acta Cryst. D62, 859-866.
17. Morishita, R., Kawagoshi, A., Sawasaki, T., Madin, K., Ogasawara, T., Oka, T. & Endo, Y. (1999). J. Biol. Chem. 274, 20688-20692.
18. Mukherjee, T., Zhang, Y., Abdelwahed, S., Ealick, S. E. & Begley, T. P. (2010). J. Am. Chem. Soc. 132, 5550-5551.
19. Murshudov, G. N., Skubá k, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
20. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Acta Cryst. D53, 240-255.
21. Oka, T., Tsuji, H., Noda, C., Sakai, K., Hong, Y., Suzuki, I.,Munoz, S. & Natori, Y. (1995). J. Biol. Chem. 270, 30060-30067.
22. Otwinowski, Z. (1991). Proceedings of the CCP4 Study Weekend. Isomorphous Replacement and Anomalous Scattering, edited by W. Wolf, P. R. Evans & A. G. W. Leslie, pp. 80-86. Warrington: Daresbury Laboratory.
23. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
24. Parsons, L., Bonander, N., Eisenstein, E., Gilson, M., Kairys, V. & Orban, J. (2002). Biochemistry, 42, 80-89.
25. Perrakis, A., Morris, R. & Lamzin, V. S. (1999). Nature Struct. Biol. 6, 458-463.
26. Rappu, P., Shin, B. S., Zalkin, H. & Mäntsälä, P. (1999). J. Bacteriol. 181, 3810- 3815.
27. Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.
28. Shimada, T., Hirao, K., Kori, A., Yamamoto, K. & Ishihama, A. (2007). Mol. Microbiol. 66, 744-757.
29. Sinha, S., Rappu, P., Lange, S. C., Mäntsälä, P., Zalkin, H. & Smith, J. L. (1999). Proc. Natl Acad. Sci. USA, 96, 13074-13079.
30. Terwilliger, T. C. (2002). Acta Cryst. D58, 1937-1940.
31. Terwilliger, T. C. & Berendzen, J. (1999). Acta Cryst. D55, 849-861.
32. Thakur, K. G., Praveena, T. & Gopal, B. (2010). Proteins, 78, 773-778.
33. Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). Nucleic Acids Res. 22, 4673-4680.
34. Tuntufye, H. N., Lebeer, S., Gwakisa, P. S. & Goddeeris, B. M. (2012). Appl. Environ. Microbiol. 78, 3343-3351.
35. Volz, K. (1999). Protein Sci. 8, 2428-2437.
36. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
37. Yang, H., Guranovic, V., Dutta, S., Feng, Z., Berman, H. M. &Westbrook, J. D. (2004). Acta Cryst. D60, 1833-1839.