Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 3, 2014, Pages 676-684

  Malecki, Piotr H ^a   Vorgias, Constantinos E ^b   Petoukhov, Maxim V ^c   Svergun, Dmitri I ^c   Rypniewski, Wojciech ^a  

^a INSTITUTE OF BIOORGANIC CHEMISTRY   (Poland)

^b UNIVERSITY OF ATHENS   (Greece)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Chitin; Chitin binding domain; Chitinase; Flexibility; Hinge regions; Ig like domain; Ligand binding; Multi domain; Psychrophilic; SAXS; TIM barrel

Indexed keywords

CHITIN; CHITINASE; CHITOTETROSE; LIGAND; OLIGOSACCHARIDE;

ARTICLE; CHEMISTRY; CHITIN-BINDING DOMAIN; ENZYME SPECIFICITY; ENZYMOLOGY; FLEXIBILITY; GENETICS; HINGE REGIONS; IG-LIKE DOMAIN; LIGAND BINDING; METABOLISM; MORITELLA; MULTI-DOMAIN; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PSYCHROPHILIC; SAXS; SMALL ANGLE SCATTERING; SOLUTION AND SOLUBILITY; TIM Β/Α-BARREL; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

CHITIN; CHITIN-BINDING DOMAIN; CHITINASE; FLEXIBILITY; HINGE REGIONS; IG-LIKE DOMAIN; LIGAND BINDING; MULTI-DOMAIN; PSYCHROPHILIC; SAXS; TIM Β/Α-BARREL;

CHITINASE; CRYSTALLOGRAPHY, X-RAY; LIGANDS; MORITELLA; OLIGOSACCHARIDES; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SCATTERING, SMALL ANGLE; SOLUTIONS; SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

EID: 84896777883     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004713032264     Document Type: Article

References (31)

1. Aalten, D. M. F. van, Komander, D., Synstad, B., Ga° seidnes, S., Peter, M. G. & Eijsink, V. G. H. (2001). Proc. Natl Acad. Sci. USA, 98, 8979-8984.
2. Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H. & Adams, P. D. (2012). Acta Cryst. D68, 352-367.
3. Akagi, K., Watanabe, J., Hara, M., Kezuka, Y., Chikaishi, E., Yamaguchi, T., Akutsu, H., Nonaka, T., Watanabe, T. & Ikegami, T. (2006). J. Biochem. 139, 483-493.
4. Bernadó , P. (2010). Eur. Biophys. J. 39, 769-780.
5. Bernadó , P., Mylonas, E., Petoukhov, M. V., Blackledge, M. & Svergun, D. I. (2007). J. Am. Chem. Soc. 129, 5656-5664.
6. Blanchet, C. E., Zozulya, A. V., Kikhney, A. G., Franke, D., Konarev, P. V., Shang,W., Klaering, R., Robrahn, B., Hermes, C., Cipriani, F., Svergun, D. I. & Roessle, M. (2012). J. Appl. Cryst. 45, 489-495.
7. Cantarel, B. L., Coutinho, P. M., Rancurel, C., Bernard, T., Lombard, V. & Henrissat, B. (2009). Nucleic Acids Res. 37, D233-D238.
8. Davies, G. & Henrissat, B. (1995). Structure, 3, 853-859.
9. Edelheit, O., Hanukoglu, A. & Hanukoglu, I. (2009). BMC Biotechnol. 9, 61.
10. Franke, D., Kikhney, A. G. & Svergun, D. I. (2012). Nucl. Instrum. Methods Phys. Res. A, 689, 52-59.
11. Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D. & Bairoch, A. (2005). The Proteomics Protocols Handbook, edited by J. M. Walker, pp. 571-607. Totowa: Humana Press.
12. Henrissat, B. & Davies, G. (1997). Curr. Opin. Struct. Biol. 7, 637-644.
13. Horn, S. J., Sikorski, P., Cederkvist, J. B., Vaaje-Kolstad, G., Sørlie,M., Synstad, B., Vriend, G., Va°rum, K. M. & Eijsink, V. G. (2006). Proc. Natl Acad. Sci. USA, 103, 18089-18094.
14. Kabsch, W. (2010). Acta Cryst. D66, 125-132.
15. Laemmli, U. K. (1970). Nature (London), 227, 680-685.
16. Malecki, P. H., Raczynska, J. E., Vorgias, C. E. & Rypniewski, W. (2013). Acta Cryst. D69, 821-829.
17. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C. & Read, R. J. (2007). J. Appl. Cryst. 40, 658-674.
18. Morita, R. Y. & Haight, R. D. (1964). Limnol. Oceanogr. 9, 103-106.
19. Papanikolau, Y., Prag, G., Tavlas, G., Vorgias, C. E., Oppenheim, A. B. & Petratos, K. (2001). Biochemistry, 40, 11338-11343.
20. Payne, C. M., Baban, J., Horn, S. J., Backe, P. H., Arvai, A. S., Dalhus, B., Bjøräs, M., Eijsink, V. G., Sørlie, M., Beckham, G. T. & Vaaje- Kolstad, G. (2012). J. Biol. Chem. 287, 36322-36330.
21. Petoukhov, M. V., Franke, D., Shkumatov, A. V., Tria, G., Kikhney, A. G., Gajda, M., Gorba, C., Mertens, H. D. T., Konarev, P. V. & Svergun, D. I. (2012). J. Appl. Cryst. 45, 342-350.
22. Poole, K. & Hancock, R. E. (1984). Eur. J. Biochem. 144, 607-612.
23. Round, A. R., Franke, D., Moritz, S., Huchler, R., Fritsche, M., Malthan, D., Klaering, R., Svergun, D. I. & Roessle, M. (2008). J. Appl. Cryst. 41, 913-917.
24. Songsiriritthigul, C., Pantoom, S., Aguda, A. H., Robinson, R. C. & Suginta, W. (2008). J. Struct. Biol. 162, 491-499.
25. Stefanidi, E. & Vorgias, C. E. (2008). Extremophiles, 12, 541-552.
26. Suzuki, K., Taiyoji, M., Sugawara, N., Nikaidou, N., Henrissat, B. & Watanabe, T. (1999). Biochem. J. 343, 587-596.
27. Svergun, D. I. (1992). J. Appl. Cryst. 25, 495-503.
28. Svergun, D., Barberato, C. & Koch, M. H. J. (1995). J. Appl. Cryst. 28, 768-773.
29. Toratani, T., Kezuka, Y., Nonaka, T., Hiragi, Y. & Watanabe, T. (2006). Biochem. Biophys. Res. Commun. 348, 814-818.
30. Tsuji, H., Nishimura, S., Inui, T., Kado, Y., Ishikawa, K., Nakamura, T. & Uegaki, K. (2010). FEBS J. 277, 2683-2695.
31. Vaaje-Kolstad, G., Horn, S. J., van Aalten, D. M. F., Synstad, B. & Eijsink, V. G. H. (2005). J. Biol. Chem. 280, 28492-28497.