Cobalt-, zinc- and iron-bound forms of adenylate kinase (AK) from the sulfate-reducing bacterium Desulfovibrio gigas: Purification, crystallization and preliminary X-ray diffraction analysis

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 65, Issue 9, 2009, Pages 926-929

  Kladova, A V ^a   Gavel, O Yu ^a,b   Mukhopaadhyay, A ^a   Boer, D R ^a   Teixeira, S ^a   Shnyrov, V L ^b   Moura, I ^a   Moura, J J G ^a   Romao M J ^a   Trincao J ^a   Bursakov, S A ^a,c  

^a UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^b UNIVERSITY OF SALAMANCA   (Spain)

^c CSIC   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); DESULFOVIBRIO GIGAS; NEGIBACTERIA; VIBRIO;

ADENYLATE KINASE; COBALT; IRON; SULFATE; ZINC;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; DESULFOVIBRIO GIGAS; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; OXIDATION REDUCTION REACTION; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

ADENYLATE KINASE; COBALT; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DESULFOVIBRIO GIGAS; IRON; OXIDATION-REDUCTION; SULFATES; X-RAY DIFFRACTION; ZINC;

EID: 69849114877     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309109029157     Document Type: Article

References (20)

1. Bae, E. & Phillips, G. N. Jr (2004). J. Biol. Chem. 279, 28202-28208
2. Berry, M. B. & Phillips, G. N. Jr (1998). Proteins, 32, 276-288
3. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763
4. Criswell, A. R., Bae, E., Stec, B., Konisky, J. & Philips, G. N. Jr (2003). J. Mol. Biol. 330, 1087-1099
5. Fenton, D. E., Schroeder, R. R. & Lintvedt, R. L. (1978). J. Am. Chem. Soc. 100, 1932-1934
6. Gavel, O. Yu., Bursakov, S. A., Di Rocco, G., Trincao, J., Pickering, I. J., George, G. N., Calvete, J. J., Shnyrov, V. L., Brondino, C. D., Pereira, A. S., Lampreia, J., Tavares, P., Moura, J. J. G. & Moura, I. (2008). J. Inorg. Biochem. 102,1380-1395
7. Gavel, O. Yu., Bursakov, S. A., Pina, D. G., Zhadan, G. G., Moura, J. J. G., Moura, I. & Shnyrov, V. L. (2004). Biophys. Chem. 110, 83-92
8. Gilles, A. M., Glaser, P., Perrier, V., Meier, A., Longin, R., Sebald, M., Maignan, L., Pistotnik, E. & Barzu, O. (1994). J. Bacteriol. 176, 520-523
9. Henzler-Wildman, K. A., Thai, V., Lei, M., Ott, M., Wolf-Watz, M., Fenn, T., Pozharski, E., Wilson, M. A., Petsko, G. A., Karplus, M., Hubner, C. G. & Kern, D. (2007). Nature (London), 450, 838-844
10. Jancarik, J. & Kim, S.-H. (1991). J. Appl. Cryst. 24, 409-411
11. Laemmli, U. K. (1970). Nature (London), 227, 680-685
12. LeGall, J., Mazza, G. & Dragoni, N. (1965). Biochim. Biophys. Acta, 99, 385-387
13. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497
14. Müller, C. W., Schlauderer, G. J., Reinstein, J. & Schulz, G. E. (1996). Structure, 4, 147-156
15. Perrier, V., Barlacu-Miron, S., Boussac, A., Meier, A. & Gilles, A. M. (1998). Protein Eng. 11, 917-923
16. Schulz, G. E. (1992). Curr. Opin. Struct. Biol. 2, 61-67
17. Vielle, C., Krishnamurthy, H., Hyun, H.-H., Savchenko, A., Yan, H. & Zeikus, G. (2003). Biochem. J. 372, 577-585
18. Vornhein, C., Bonisch, H., Schafer, G. & Schulz, G. E. (1998). J. Mol. Biol. 282, 167-179
19. Weiss, M. S. (2001). J. Appl. Cryst. 34, 130-135
20. Yan, H. & Tsai, M. D. (1999). Adv. Enzymol. Relat. Areas Mol. Biol. 73, 103-134.