Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit €

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 10, 2012, Pages 1229-1233

  Roy, Ankoor ^a   Hutcheon, Marcus L ^b   Duncan, Thomas M ^b   Cingolani, Gino ^a  

^a THOMAS JEFFERSON UNIVERSITY   (United States)

^b State University of New York Upstate Medical University: College of Medicine   (United States)

Author keywords

Crystallization; FOF1 ATP synthase; phosphomimetic mutation; subunit

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

ARTICLE; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; MUTATION; PROTEIN SUBUNIT; PROTEIN TERTIARY STRUCTURE;

ADENOSINE TRIPHOSPHATASES; BIOCATALYSIS; CRYSTALLIZATION; ESCHERICHIA COLI; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS;

EID: 84867254749     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112036718     Document Type: Article

References (26)

1. Abrahams, J. P., Leslie, A. G., Lutter, R. & Walker, J. E. (1994). Nature (London), 370, 621-628.
2. Borsch, M. (2011). Biol. Chem. 392, 135-142.
3. Bowler, M. W., Montgomery, M. G., Leslie, A. G. & Walker, J. E. (2007). J. Biol. Chem. 282, 14238-14242.
4. Cingolani, G. & Duncan, T. M. (2011). Nat. Struct. Mol. Biol. 18, 701-707.
5. Duncan, T. M. (2004). The Enzymes, Vol. 23, Energy Coupling and Molecular Motors, edited by D. D. Hackney & F. Tamanoi, pp. 203-275. New York: Academic Press.
6. Duncan, T. M., Bulygin, V. V., Zhou, Y., Hutcheon, M. L. & Cross, R. L. (1995). Proc. Natl Acad. Sci. USA, 92, 10964-10968.
7. Duncan, T. M., Zhou, Y., Bulygin, V. V., Hutcheon, M. L. & Cross, R. L. (1995). Biochem. Soc. Trans. 23, 736-741.
8. Feniouk, B. A., Suzuki, T. & Yoshida, M. (2006). Biochim. Biophys. Acta, 1757, 326-338.
9. Gibbons, C., Montgomery, M. G., Leslie, A. G. & Walker, J. E. (2000). Nat. Struct. Biol. 7, 1055-1061.
10. Gibson, F. (2000). Trends Biochem. Sci. 25, 342-344.
11. Hausrath, A. C., Capaldi, R. A. & Matthews, B. W. (2001). J. Biol. Chem. 276, 47227-47232.
12. Hausrath, A. C., Gruber, G., Matthews, B. W. & Capaldi, R. A. (1999). Proc. Natl Acad. Sci. USA, 96, 13697-13702.
13. Kabaleeswaran, V., Puri, N., Walker, J. E., Leslie, A. G. & Mueller, D. M. (2006). EMBO J. 25, 5433-5442.
14. Noji, H., Okuno, D. & Ikeda, T. (2011). Chem. Sci. 2, 2086-2093.
15. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
16. Peterson, G. L. (1977). Anal. Biochem. 83, 346-356.
17. Pullman, M. E., Penefsky, H. S., Datta, A. & Racker, E. (1960). J. Biol. Chem. 235, 3322-3329.
18. Schaefer, E. M., Hartz, D., Gold, L. & Simoni, R. D. (1989). J. Bacteriol. 171, 3901-3908.
19. Senior, A. E., Fayle, D. R., Downie, J. A., Gibson, F. & Cox, G. B. (1979). Biochem. J. 180, 111-118.
20. Stock, D., Leslie, A. G. & Walker, J. E. (1999). Science, 286, 1700-1705.
21. Stocker, A., Keis, S., Vonck, J., Cook, G. M. & Dimroth, P. (2007). Structure, 15, 904-914.
22. Uhlin, U., Cox, G. B. & Guss, J. M. (1997). Structure, 5, 1219-1230.
23. Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. & Walker, J. E. (2010). Proc. Natl Acad. Sci. USA, 107, 16823-16827.
24. Wilkens, S. & Capaldi, R. A. (1998). J. Biol. Chem. 273, 26645-26651.
25. Wise, J. G. (1990). J. Biol. Chem. 265, 10403-10409.
26. Yagi, H., Kajiwara, N., Tanaka, H., Tsukihara, T., Kato-Yamada, Y., Yoshida, M. & Akutsu, H. (2007). Proc. Natl Acad. Sci. USA, 104, 11233-11238.