The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 67, Issue 2, 2011, Pages 193-200

  Gaur, Vineet ^a   Chanana, Veenu ^a   Jain, Abha ^a   Salunke, Dinakar M ^a,b  

^a NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

^b REGIONAL CENTRE FOR BIOTECHNOLOGY   (India)

Author keywords

CP4; Haemopexin fold; Vigna unguiculata

Indexed keywords

HEME; HEMOPEXIN; PROTEIN SUBUNIT; PROTEOME; SPERMINE; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CALIBRATION; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; CRYSTALLIZATION; DIMERIZATION; HYDROLYSIS; ISOLATION AND PURIFICATION; LATHYRUS; LEGUME; MACROMOLECULE; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; PEA; PLANT; PLANT SEED; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STANDARD; X RAY CRYSTALLOGRAPHY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BASE SEQUENCE; CALIBRATION; CONSERVED SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FABACEAE; HEME; HEMOPEXIN; HYDROLYSIS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LATHYRUS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PEAS; PLANT PROTEINS; PLANTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTEOME; REFERENCE STANDARDS; SEEDS; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE HOMOLOGY, AMINO ACID; SPERMINE;

ANIMALIA; LATHYRUS SATIVUS; MAMMALIA; PISUM SATIVUM; VIGNA UNGUICULATA;

EID: 79951485050     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309110051250     Document Type: Article

References (34)

1. Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W. &Lipman, D. J. (1997). Nucleic Acids Res. 25, 3389-3402.
2. Bertini, I., Calderone, V., Fragai, M., Jaiswal, R., Luchinat, C., Melikian, M., Mylonas, E. &Svergun, D. I. (2008). J. Am. Chem. Soc. 130, 7011-7021.
3. Blancher, C., Omri, B., Bidou, L., Pessac, B. &Crisanti, P. (1996). J. Biol. Chem. 271, 26220-26226.
4. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. &Warren, G. L. (1998). Acta Cryst. D54, 905-921.
5. Chanana, V., Kaur, K. J. &Salunke, D. M. (2004). Acta Cryst. D60, 2100-2103.
6. Crennell, S. J., Tickler, P. M., Bowen, D. J. &ffrench-Constant, R. H. (2000). FEMS Microbiol. Lett. 191, 139-144.
7. Croy, R. R., Hoque, M. S., Gatehouse, J. A. &Boulter, D. (1984). Biochem. J. 218, 795-803.
8. Emsley, P. &Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
9. Faber, H. R., Groom, C. R., Baker, H. M., Morgan, W. T., Smith, A. &Baker, E. N. (1995). Structure, 3, 551-559.
10. Fülöp, V. &Jones, D. T. (1999). Curr. Opin. Struct. Biol. 9, 715-721.
11. Gaur, V., Qureshi, I. A., Singh, A., Chanana, V. &Salunke, D. M. (2010). Plant Physiol. 152, 1842-1850.
12. Gomis-Ruth, F. X., Gohlke, U., Betz, M., Knauper, V., Murphy, G., Lopez-Otin, C. &Bode, W. (1996). J. Mol. Biol. 264, 556-566.
13. Gruen, L. C., Guthrie, R. E. &Blagrove, R. J. (1987). J. Sci. Food Agric. 41, 167-178.
14. Harris, N. &Croy, R. R. D. (1985). Planta, 165, 522-526.
15. Higgins, T. J. V., Beach, L. R., Spencer, D., Chandler, P. M., Randall, P. J., Blagrove, R. J., Kortt, A. A. &Guthrie, R. E. (1987). Plant Mol. Biol. 8, 37-45.
16. Hrkal, Z., Vodrazka, Z. &Kalousek, I. (1974). Eur. J. Biochem. 43, 73-78.
17. Iyer, S., Visse, R., Nagase, H. &Acharya, K. R. (2006). J. Mol. Biol. 362, 78-88.
18. Jenne, D. (1991). Biochem. Biophys. Res. Commun. 176, 1000-1006.
19. Jozic,D., Bourenkov, G., Lim, N.-H., Visse, R., Nagase, H., Bode,W. &Maskos, K. (2005). J. Biol. Chem. 280, 9578-9585.
20. Kolberg, J., Michaelsen, T. E. &Sletten, K. (1983). Hoppe Seylers Z. Physiol. Chem. 364, 655-664.
21. Landschulz,W. H., Johnson, P. F. &McKnight, S. L. (1988). Science, 240, 1759-1764.
22. Laskowski, R. A., MacArthur, M. W., Moss, D. S. &Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
23. Libson, A. M., Gittis, A. G., Collier, I. E., Marmer, B. L., Goldberg, G. I. &Lattman, E. E. (1995). Nature Struct. Biol. 2, 938-942.
24. Liu, T., Lin, Y., Cislo, T., Minetti, C. A., Baba, J. M. &Liu, T.-Y. (1991). J. Biol. Chem. 266, 14813-14821.
25. Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S. &Dodson, E. J. (1999). Acta Cryst. D55, 247-255.
26. Navaza, J. (2001). Acta Cryst. D57, 1367-1372.
27. Paoli, M., Anderson, B. F., Baker, H. M., Morgan, W. T., Smith, A. &Baker, E. N. (1999). Nature Struct. Biol. 6, 926-931.
28. Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C. &Ferrin, T. E. (2004). J. Comput. Chem. 25, 1605-1612.
29. Piccard, H., Van den Steen, P. E. &Opdenakker, G. (2007). J. Leukoc. Biol. 81, 870-892.
30. Qureshi, I. A., Sethi, D. K. &Salunke, D. M. (2006). Acta Cryst. F62, 869-872.
31. Thompson, J. D., Higgins, D. G. &Gibson, T. J. (1994). Nucleic Acids Res. 22, 4673-4680.
32. Vigeolas, H., Chinoy, C., Zuther, E., Blessington, B., Geigenberger, P. &Domoney, C. (2008). Plant Physiol. 146, 74-82.
33. Vioque, J., Clemente, A., Sánchez-Vioque, R., Pedroche, J., Bautista, J. &Millán, F. (1998). J. Agric. Food Chem. 46, 3609-3613.
34. Winn, M. D., Isupov, M. N. &Murshudov, G. N. (2001). Acta Cryst. D57, 122-133.