Crystal structure of the protealysin precursor: Insights into propeptide function

Journal of Biological Chemistry

Volumn 285, Issue 3, 2010, Pages 2003-2013

  Demidyuk, Ilya V ^a   Gromova, Tania Yu ^a   Polyakov, Konstantin M ^b   Melik Adamyan, William R ^c   Kuranova, Inna P ^c   Kostrov, Sergey V ^a  

^a INSTITUTE OF MOLECULAR GENETICS   (Russian Federation)

^b KURCHATOV INSTITUTE   (Russian Federation)

^c SHUBNIKOV INSTITUTE OF CRYSTALLOGRAPHY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE CENTER; ACTIVE SITE; CALCIUM BINDING; CATALYTIC DOMAINS; CRITICAL ELEMENTS; DIFFERENT STRUCTURE; N-TERMINALS; PRIMARY STRUCTURES; PROPEPTIDES; SECOND GROUP; SUBSITES; SUBSTRATE-BINDING SITES; THERMOLYSIN; THREE-DIMENSIONAL STRUCTURE;

AMINO ACIDS; BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; CALCIUM; CATALYSTS; ENZYMES; ORGANIC ACIDS; THREE DIMENSIONAL;

CRYSTAL STRUCTURE;

PEPTIDASE; PROTEALYSIN PRECURSOR; UNCLASSIFIED DRUG; ENZYME PRECURSOR; METALLOPROTEINASE; MICROBIAL METALLOPROTEINASES;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN MOTIF; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME PRECURSORS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA;

EID: 76249091390     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.015396     Document Type: Article

References (52)

1. Rawlings, N. D., and Barrett, A. J. (1995) Methods Enzymol. 248, 183-228
2. Rawlings, N. D., Morton, F. R., Kok, C. Y., Kong, J., and Barrett, A. J. (2008) Nucleic Acids Res. 36, D320-325
3. Adekoya, O. A., and Sylte, I. (2009) Chem. Biol. Drug. Des. 73, 7-16
4. Titani, K., Hermodson, M. A., Ericsson, L. H., Walsh, K. A., and Neurath, H. (1972) Biochemistry 11, 2427-2435
5. Matthews, B. W., Jansonius, J. N., Colman, P. M., Schoenborn, B. P., and Dupourque, D. (1972) Nature New. Biol. 238, 37-41
6. Pauptit, R. A., Karlsson, R., Picot, D., Jenkins, J. A., Niklaus-Reimer, A. S., and Jansonius, J. N. (1988) J. Mol. Biol. 199, 525-537
7. Stark, W., Pauptit, R. A., Wilson, K. S., and Jansonius, J. N. (1992) Eur. J. Biochem. 207, 781-791
8. Thayer, M. M., Flaherty, K. M., and McKay, D. B. (1991) J. Biol. Chem. 266, 2864-2871
9. Banbula, A., Potempa, J., Travis, J., Fernandez-Catalán, C., Mann, K., Huber, R., Bode, W., and Medrano, F. (1998) Structure 6, 1185-1193
10. Demidyuk, I. V., Gasanov, E. V., Safina, D. R., and Kostrov, S. V. (2008) Protein J. 27, 343-354
11. McIver, K. S., Kessler, E., Olson, J. C., and Ohman, D. E. (1995) Mol. Microbiol. 18, 877-889
12. Braun, P., Tommassen, J., and Filloux, A. (1996) Mol. Microbiol. 19, 297-306
13. Marie-Claire, C., Ruffet, E., Beaumont, A., and Roques, B. P. (1999) J. Mol. Biol. 285, 1911-1915
14. Tang, B., Nirasawa, S., Kitaoka, M., Marie-Claire, C., and Hayashi, K. (2003) Biochem. Biophys. Res. Commun. 301, 1093-1098
15. Kessler, E., and Safrin, M. (1994) J. Biol. Chem. 269, 22726-22731
16. O'Donohue, M. J., and Beaumont, A. (1996) J. Biol. Chem. 271, 26477-125481
17. Serkina, A. V., Gorozhankina, T. F., Shevelev, A. B., and Chestukhina, G. G. (1999) FEBS Lett. 456, 215-219
18. Wetmore, D. R., Wong, S. L., and Roche, R. S. (1992) Mol. Microbiol. 6, 1593-1604
19. Demidyuk, I. V., Kalashnikov, A. E., Gromova, T. Y., Gasanov, E. V., Safina, D. R., Zabolotskaya, M. V., Rudenskaya, G. N., and Kostrov, S. V. (2006) Protein. Expr. Purif. 47, 551-561
20. Gromova, T., Demidyuk, I., Kostrov, S., Sosfenov, N., Melik-Adamyan, V., and Kuranova, I. (2008) Crystallogr. Rep. 53, 793-795
21. Gromova, T. Y., Demidyuk, I. V., Kozlovskiy, V. I., Kuranova, I. P., and Kostrov, S. V. (2009) Biochimie 91, 639-645
22. Dodonov, A. F., Loboda, A. V., Kozlovski, V. I., Soulimenkov, I. V., Raznikov, V. V., Zhen, Z., Horwath, T., and Wollnik, H. (2000) Eur. J. Mass Spectro. 6, 481-490
23. Kheiker, D., Kovalchuk, M., Shilin, Y., Shishkov, V., Sulyanov, S., Dorovatovskii, P., and Rusakov, A. (2007) Crystallogr. Rep. 52, 358-364
24. Kabsch, W. (1993) J. Appl. Crystallogr. 26, 795-800
25. Long, F., Vagin, A. A., Young, P., and Murshudov, G. N. (2008) Acta Crystallogr. D Biol. Crystallogr. 64, 125-132
26. Vagin, A., and Teplyakov, A. (1997) J. Appl. Crystallogr. 30, 1022-1025
27. (1994) Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
28. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. D Biol. Crystallogr. 53, 240-255
29. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
30. Read, R. J. (1986) Acta Crystallogr. Sect. A 42, 140-149
31. Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) Nucleic Acids Res. 25, 4876-4882
32. Schneider, T. D., and Stephens, R. M. (1990) Nucleic Acids Res. 18, 6097-6100
33. Crooks, G. E., Hon, G., Chandonia, J. M., and Brenner, S. E. (2004) Genome Res. 14, 1188-1190
34. Guex, N., and Peitsch, M. C. (1997) Electrophoresis 18, 2714-2723
35. DeLano, W. L. (2007) The PyMOL Molecular Graphics System, DeLano Scientific LLC, San Carlos, CA
36. Dahlquist, F. W., Long, J. W., and Bigbee, W. L. (1976) Biochemistry 15, 1103-1111
37. Roche, R. S., and Voordouw, G. (1978) CRC Crit. Rev. Biochem. 5, 1-23
38. Corbett, R. J., and Roche, R. S. (1983) Biopolymers 22, 101-105
39. Veltman, O. R., Vriend, G., Berendsen, H. J., Van den Burg, B., Venema, G., and Eijsink, V. G. (1998) Biochemistry 37, 5312-5319
40. Schechter, I., and Berger, A. (1967) Biochem. Biophys. Res. Commun. 27, 157-162
41. Tsaplina, O. A., Efremova, T. N., Kever, L. V., Komissarchik, Y. Y., Demidyuk, I. V., Kostrov, S. V., and Khaitlina, S. Y. (2009) Biochemistry 74, 648-654
42. Khaitlina, SYu, Smirnova, T. D., and Usmanova, A. M. (1988) FEBS Lett. 228, 172-174
43. Bozhokina, E., Khaitlina, S., and Adam, T. (2008) Biochem. Biophys. Res. Commun. 367, 888-892
44. McKay, D. B., Thayer, M. M., Flaherty, K. M., Pley, H., and Benvegnu, D. (1992) Matrix Suppl. 1, 112-115
45. Hausrath, A. C., and Matthews, B. W. (2002) Acta Crystallogr. D Biol. Crystallogr. 58, 1002-1007
46. Holland, D. R., Tronrud, D. E., Pley, H. W., Flaherty, K. M., Stark, W., Jansonius, J. N., McKay, D. B., and Matthews, B. W. (1992) Biochemistry 31, 11310-11316
47. Hangauer, D. G., Monzingo, A. F., and Matthews, B. W. (1984) Biochemistry 23, 5730-5741
48. Matthews, B. W. (1988) Acc. Chem. Res. 21, 333-340
49. Feder, J. (1967) Biochemistry 6, 2088-2093
50. Feder, J., and Schuck, J. M. (1970) Biochemistry 9, 2784-2791
51. Diederichs, K., and Karplus, P. A. (1997) Nat. Struct. Biol. 4, 269-275
52. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., 3rd, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) Nucleic Acids Res. 35, W375-383