Crystal structure and mutational analysis of aminoacylhistidine dipeptidase from Vibrio alginolyticus reveal a new architecture of M20 metallopeptidases

Journal of Biological Chemistry

Volumn 285, Issue 50, 2010, Pages 39500-39510

  Chang, Chin Yuan ^a   Hsieh, Yin Cheng ^b,c   Wang, Ting Yi ^a   Chen, Yi Chin ^a   Wang, Yu Kuo ^a   Chiang, Ting Wei ^b,c   Chen, Yi Ju ^a   Chang, Cheng Hsiang ^a   Chen, Chun Jung ^b,c,d   Wu, Tung Kung ^a,e  

^a NATIONAL CHIAO TUNG UNIVERSITY   (Taiwan)

^b NATIONAL SYNCHROTRON RADIATION RESEARCH CENTER   (Taiwan)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^d NATIONAL CHENG KUNG UNIVERSITY   (Taiwan)

^e NONE   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINOBUTYRIC ACIDS; BELONG TO; CARNOSINE; CATALYTIC DOMAINS; DIMER INTERFACE; DIMERIC STRUCTURE; DIPEPTIDE; GABAERGIC; HOMODIMERS; METALLOPEPTIDASES; MUTATIONAL ANALYSIS; NEUROPROTECTION; POLYPEPTIDE CHAIN; POTENTIAL VALUES; SUBSTRATE RECOGNITION; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING; TRIPEPTIDE; VIBRIO ALGINOLYTICUS; WILD TYPES; ZINC IONS;

AMINO ACIDS; CRYSTAL STRUCTURE; DIMERS; HYDROGEN BONDS; MONOMERS; TOPOLOGY; ZINC;

SUBSTRATES;

AMINOACYLHISTIDINE DIPEPTIDASE; M20 METALLOPEPTIDASE; METALLOPROTEINASE; PROTEINASE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROLYSIS; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURAL HOMOLOGY; VIBRIO ALGINOLYTICUS;

AMINO ACIDS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDASES; DNA MUTATIONAL ANALYSIS; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYDROGEN BONDING; KINETICS; MOLECULAR CONFORMATION; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; VIBRIO ALGINOLYTICUS;

VIBRIO ALGINOLYTICUS;

EID: 78649806126     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.139683     Document Type: Article

References (47)

1. Chen, S. L., Marino, T., Fang, W. H., Russo, N., and Himo, F. (2008) J. Phys. Chem. B 112, 2494-2500
2. Vongerichten, K. F., Klein, J. R., Matern, H., and Plapp, R. (1994) Microbiology 140, 2591-2600
3. Hellendoorn, M. A., Franke-Fayard, B. M., Mierau, I., Venema, G., and Kok, J. (1997) J. Bacteriol. 179, 3410-3415
4. Biagini, A., and Puigserver, A. (2001) Comp. Biochem. Physiol. B Biochem. Mol. Biol. 128, 469-481
5. Bommarius, A. S. (2002) in Enzyme Catalysis in Organic Synthesis (Drauz, K., and Waldmann, H., eds) pp. 741-749, Wiley-VCH, Weinheim
6. Jozic, D., Bourenkow, G., Bartunik, H., Scholze, H., Dive, V., Henrich, B., Huber, R., Bode, W., and Maskos, K. (2002) Structure 10, 1097-1106
7. Håkansson, K., and Miller, C. G. (2002) Eur. J. Biochem. 269, 443-450
8. Lundgren, S., Gojković, Z., Piskur, J., and Dobritzsch, D. (2003) J. Biol. Chem. 278, 51851-51862
9. Klein, J., and Henrich, B. (2004) in Handbook of Proteolytic Enzymes (Barrett, A. J., Rawlings, N. D., and Woessner, J. F., eds) 2nd Ed., pp. 948-949, Elsevier, London
10. Miller, C. G., and Boder, D. H. (2004) in Handbook of Proteolytic Enzymes (Barrett, A. J., Rawlings, N. D., and Woessner, J. F., eds) pp. 946-948, Elsevier, London
11. Agarwal, R., Burley, S. K., and Swaminathan, S. (2007) J. Mol. Biol. 368, 450-463
12. Schroeder, U., Henrich, B., Fink, J., and Plapp, R. (1994) FEMS Microbiol. Lett. 123, 153-159
13. Teufel, M., Saudek, V., Ledig, J. P., Bernhardt, A., Boularand, S., Carreau, A., Cairns, N. J., Carter, C., Cowley, D. J., Duverger, D., Ganzhorn, A. J., Guenet, C., Heintzelmann, B., Laucher, V., Sauvage, C., and Smirnova, T. (2003) J. Biol. Chem. 278, 6521-6531
14. Unno, H., Yamashita, T., Ujita, S., Okumura, N., Otani, H., Okumura, A., Nagai, K., and Kusunoki, M. (2008) J. Biol. Chem. 283, 27289-27299
15. Perry, T. L., Hansen, S., and Love, D. L. (1968) Lancet 1, 1229-1230
16. Perry, T. L., Hansen, S., Tischler, B., Bunting, R., and Berry, K. (1967) N. Engl. J. Med. 277, 1219-1227
17. Terplan, K. L., and Cares, H. L. (1972) Neurology 22, 644-655
18. Murphey, W. H., Lindmark, D. G., Patchen, L. I., Housler, M. E., Harrod, E. K., and Mosovich, L. (1973) Pediatr. Res. 7, 601-606
19. Lunde, H., Sjaastad, O., and Gjessing, L. (1982) J. Neurochem. 38, 242-245
20. Karita, M., Etterbeek, M. L., Forsyth, M. H., Tummuru, M. K., and Blaser, M. J. (1997) Infect. Immun. 65, 4158-4164
21. Minton, N. P., Atkinson, T., Bruton, C. J., and Sherwood, R. F. (1984) Gene 31, 31-38
22. Sherwood, R. F., Melton, R. G., Alwan, S. M., and Hughes, P. (1985) Eur. J. Biochem. 148, 447-453
23. Rowsell, S., Pauptit, R. A., Tucker, A. D., Melton, R. G., Blow, D. M., and Brick, P. (1997) Structure 5, 337-347
24. Khan, T. H., Eno-Amooquaye, E. A., Searle, F., Browne, P. J., Osborn, H. M., and Burke, P. J. (1999) J. Med. Chem. 42, 951-956
25. Krause, A. S., Weihrauch, M. R., Bode, U., Fleischhack, G., Elter, T., Heuer, T., Engert, A., Diehl, V., and Josting, A. (2002) Leuk. Lymphoma 43, 2139-2143
26. Boldyrev, A. A. (2000) Biochemistry 65, 751-756
27. Vaughan, F. L., Hughes, E. A., Jones, R. S., Woods, R. T., and Tipper, S. P. (2006) J. Int. Neuropsychol. Soc. 12, 416-423
28. Decker, E. A., Livisay, S. A., and Zhou, S. (2000) Biochemistry 65, 766-770
29. Seidler, N. W. (2000) J. Biochem. Mol. Toxicol. 14, 215-220
30. Guiotto, A., Calderan, A., Ruzza, P., and Borin, G. (2005) Curr. Med. Chem. 12, 2293-2315
31. Hipkiss, A. R. (1998) Int. J. Biochem. Cell Biol. 30, 863-868
32. Tabakman, R., Lazarovici, P., and Kohen, R. (2002) J. Neurosci. Res. 68, 463-469
33. Petroff, O. A., Hyder, F., Mattson, R. H., and Rothman, D. L. (1999) Neurology 52, 473-478
34. Petroff, O. A., Hyder, F., Rothman, D. L., and Mattson, R. H. (2001) Neurology 56, 709-715
35. Sauerhöfer, S., Yuan, G., Braun, G. S., Deinzer, M., Neumaier, M., Gretz, N., Floege, J., Kriz, W., van der Woude, F., and Moeller, M. J. (2007) Diabetes 56, 2425-2432
36. Wang, T. Y., Chen, Y. C., Kao, L. W., Chang, C. Y., Wang, Y. K., Liu, Y. H., Feng, J. M., and Wu, T. K. (2008) FEBS J. 275, 5007-5020
37. Chang, C. Y., Hsieh, Y. C., Wang, T. Y., Chen, C. J., and Wu, T. K. (2009) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65, 216-218
38. Chevrier, B., Schalk, C., D'Orchymont, H., Rondeau, J. M., Moras, D., and Tarnus, C. (1994) Structure 2, 283-291
39. Greenblatt, H. M., Almog, O., Maras, B., Spungin-Bialik, A., Barra, D., Blumberg, S., and Shoham, G. (1997) J. Mol. Biol. 265, 620-636
40. Lindner, H. A., Lunin, V. V., Alary, A., Hecker, R., Cygler, M., and Ménard, R. (2003) J. Biol. Chem. 278, 44496-44504
41. Csámpai, A., Kutlán, D., Tóth, F., and Molnár-Perl, I. (2004) J. Chromatogr. A 1031, 67-78
42. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
43. Weiss, M. S. (2001) J. Appl. Cryst. 34, 130-135
44. Evans, P. (2006) Acta Crystallogr. D Biol. Crystallogr. 62, 72-82
45. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
46. Lovell, S. C., Davis, I. W., Arendall, W. B., 3rd, de Bakker, P. I., Word, J. M., Prisant, M. G., Richardson, J. S., and Richardson, D. C. (2003) Proteins 50, 437-450
47. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Cryst. 26, 283-291