NarL dimerization? Suggestive evidence from a new crystal form

Biochemistry

Volumn 37, Issue 11, 1998, Pages 3665-3676

  Baikalov, Igor ^a   Schröder, Imke ^a   Kaczor Grzeskowiak, Maria ^a   Cascio, Duilio ^a   Gunsalus, Robert P ^a   Dickerson, Richard E ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ESCHERICHIA COLI; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0344813718     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972365a     Document Type: Article

References (29)

1. Baikalov, I., Schröder, I., Kaczor-Grzeskowiak, M., Grzeskowiak, K., Gunsalus, R. P., and Dickerson, R. E. (1996) Biochemistry 35, 11053-11061.
2. Tyson, K. L., Bell, A. I., Cole, J. A., and Busby, S. J. W. (1993) Mol. Microbiol. 7, 151-157.
3. Otwinowski, Z. (1993) CCP4 Daresbury Study Weekend, Daresbury Laboratory, Warrington, WA4 4AD, U.K.
4. French, S., and Wilson, K. (1978) Acta Cryslallogr. A34, 517-525.
5. Bailey, S. (1994) Acta Crystallogr. D50, 760-763.
6. Matthews, B. W. (1968) J. Mol. Biol. 33, 491-497.
7. Navaza, J. (1994) Acta Crystallogr. A50, 157-163.
8. Brünger, A. T. (1992a) X-PLOR: A system for X-ray crystallography and NMK, Yale University, New Haven, CT.
9. Engh, R. A., and Huber, R. (1991) Acta Crystallogr. A47, 392-400.
10. Brünger, A. T. (1992b) Nature 355, 472-475.
11. Kleywegt, G. J., and Jones, T. A. (1995) Structure 3, 535-540.
12. Rice, L. M., and Brünger, A. T. (1994) Proteins: Struct., Funct., Genet. 19, 277-290.
13. Jones, T. A. (1978) J. Appl. Crystallogr. 11, 268-272.
14. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thomton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
15. Rech, S., Hemschemeier, K., Jarvis, M., and Gunsalus, R. P. (1997) (in preparation).
16. Webber, C. A., and Kadner, R. J. (1997) Mol. Microbiol. 24, 1039-1048.
17. Stock, A. M., Mottonen, J. M., Stock, J. B., and Schutt, C. E. (1989) Nature 337, 745-749.
18. Volz, K., and Matsumura, P. (1991) J. Biol. Chem. 266, 15511-15519.
19. Bellsolell, L., Priet, J., Serrano, L., and Coll, M. (1994) J. Mol. Biol. 238, 489-495.
20. Ganguli, S., Wang, H., Matsumura, P., and Volz, K. (1995) J. Biol. Chem. 270, 17386-17393.
21. Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., and Petsko, G. A. (1993) Biochemistry 32, 13375-13380.
22. Sanna, M. G., Swanson, R. V., Bourret, R. B., and Simon, M. I. (1995) Mol. Microbiol. 15, 1069-1079.
23. Li, J., Kustu, S., and Stewart, V. (1994) J. Mol. Biol. 241, 150-165.
24. Wilson, D. S., Guenther, B., Desplan, C., and Kuriyan, J. (1995) Cell 82, 709-719.
25. Xu, W., Rould, M. A., Jun, S., Desplan, C., and Pabo, C. O. (1995) Cell 80, 639-650.
26. Beamer, L. J., and Pabo, C. O. (1992) J. Mol. Biol. 227, 177-196.
27. Schultz, S. C., Shields, G. C., and Steitz, T. A. (1992) Science 253, 1001-1007.
28. Parkinson, G., Wilson, C., Gunasekera, A., Ebright, Y. W., Ebright, R. H., and Berman, H. M. (1996) J. Mol. Biol. 260, 395-408.
29. Otwinowski, Z., Schevitz, R. W., Zhang, R. G., Lawson, C. L., Joachimiak, A., Marmorstein, R. Q., Luisi, B. F., and Sigler, P. B. (1988) Nature 335, 321-329.