Structural studies of hydrogen bonds in the high-affinity streptavidin-biotin complex: Mutations of amino acids interacting with the ureido oxygen of biotin

Acta Crystallographica - Section D Biological Crystallography

Volumn 59, Issue 9, 2003, Pages 1567-1573

  Le Trong, Isolde ^a   Freitag, Stefanie ^a,b   Klumb, Lisa A ^b   Chu, Vano ^b   Stayton, Patrick S ^b   Stenkamp, Ronald E ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b University of Washington   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BIOTIN; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; STREPTAVIDIN;

EID: 0042786628     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444903014562     Document Type: Article

References (26)

1. Brünger, A. T. (1992). Nature (London), 355, 472-475.
2. Chilkoti, A. & Stayton, P. S. (1995). J. Am. Chem. Soc. 117, 10622-10628.
3. Chilkoti, A., Tan, P. H. & Stayton, P. S. (1995). Proc. Natl Acad. Sci. USA, 92, 1754-1758.
4. Chu, V., Freitag, S., Le Trong, I., Stenkamp, R. E. & Stayton, P. S. (1998). Protein Sci. 7, 848-859.
5. Engh, R. A. & Huber, R. (1991). Acta Cryst. A47, 392-400.
6. Freitag, S., Le Trong, I., Chilkoti, A., Klumb, L. A., Stayton, P. S. & Stenkamp, R. E. (1998). J. Mol. Biol. 279, 211-221.
7. Freitag, S., Le Trong, I., Klumb, L., Stayton, P. S. & Stenkamp, R. E. (1997). Protein Sci. 6, 1157-1166.
8. Freitag, S., Le Trong, I., Klumb, L. A., Stayton, P. S. & Stenkamp, R. E. (1999). Acta Cryst. D55, 1118-1126.
9. Green, N. M. (1963). Biochem. J. 89, 599-609.
10. Hendrickson, W. A., Pahler, A., Smith, J. L., Satow, Y., Merritt, E. A. & Phizackerley, R. P. (1989). Proc. Natl Acad. Sci. USA, 86, 2190-2194.
11. Hyre, D. E., Le Trong, I., Freitag, S., Stenkamp, R. E. & Stayton, P. S. (2000). Protein Sci. 9, 878-885.
12. Kleywegt, G. J. & Jones, T. A. (1996). Structure, 4, 1395-1400.
13. Klumb, L. A., Chu, V. & Stayton, P. S. (1998). Biochemistry, 37, 7657-7663.
14. Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.
15. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
16. McRee, D. E. (1999). J. Struct. Biol. 125, 156-165.
17. Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.
18. Moews, P. C. & Kretsinger, R. H. (1975). J. Mol. Biol. 91, 201-228.
19. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
20. Parkin, S., Moezzi, B. & Hope, H. (1995). J. Appl. Cryst. 28, 53-56.
21. Pearlman, D. A. & Connelly, P. R. (1995). J. Mol. Biol. 248, 696-717.
22. Read, R. J. (1986). Acta Cryst. A42, 140-149.
23. Schmidt, T. G., Koepke, J., Frank, R. & Skerra, A. (1996). J. Mol. Biol. 255, 753-766.
24. Sheldrick, G. M. & Schneider, T. R. (1997). Methods Enzymol. 277, 319-343.
25. Vriend, G. & Sander, C. (1993). J. Appl. Cryst. 26, 47-60.
26. Weber, P. C., Ohlendorf, D. H., Wendoloski, J. J. & Salemme, F. R. (1989). Science, 243, 85-88.