Terminal alkene formation by the thioesterase of curacin A biosynthesis: Structure of a decarboxylating thioesterase

Journal of Biological Chemistry

Volumn 286, Issue 16, 2011, Pages 14445-14454

  Gehret, Jennifer J ^a,b   Gu, Liangcai ^a,b,e   Gerwick, William H ^c   Wipf, Peter ^d   Sherman, David H ^a,b   Smith, Janet L ^a,b  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d UNIVERSITY OF PITTSBURGH   (United States)

^e HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACYL CARRIER PROTEINS; ACYL CHAIN; ACYL-ACP; ANTICANCER PROPERTIES; ARGININE RESIDUE; ASSEMBLY LINE; BIOSYNTHETIC STRATEGIES; CATALYTIC TRIAD; LEAVING GROUPS; MACROLACTONES; MARINE CYANOBACTERIUM; NATURAL PRODUCTS; NONRIBOSOMAL PEPTIDE SYNTHETASES; OFF-LOAD; OPEN CONFORMATION; POLYKETIDE SYNTHASES; POTENTIAL VALUES; SEQUENCE IDENTITY; SUBDOMAIN; SULFATE GROUPS; TERMINAL ALKENES; THIOESTERASES;

AMINO ACIDS; ARGININE; BIOCHEMISTRY; BIOSYNTHESIS; CARBOXYLATION; CARBOXYLIC ACIDS; OLEFINS; SUBSTRATES;

CRYSTAL STRUCTURE;

ALKENE; ARGININE; CURACIN A; DIMER; GLUTAMIC ACID; HISTIDINE; HYDROLASE; POLYKETIDE SYNTHASE; SERINE; SULFATE; THIOL ESTER HYDROLASE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYANOBACTERIUM; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SYNTHESIS; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; SEQUENCE HOMOLOGY; SULFONATION;

AMINO ACID SEQUENCE; BIOFUELS; CARBOXYLIC ACIDS; CRYSTALLOGRAPHY, X-RAY; CYANOBACTERIA; CYCLOPROPANES; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PALMITOYL-COA HYDROLASE; POLYKETIDE SYNTHASES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; THIAZOLES;

BACTERIA (MICROORGANISMS); LYNGBYA MAJUSCULA;

EID: 79954598176     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.214635     Document Type: Article

References (42)

1. Newman, D. J., and Cragg, G. M. (2007) J. Nat. Prod. 70, 461-477
2. Fortman, J. L., Chhabra, S., Mukhopadhyay, A., Chou, H., Lee, T. S., Steen, E., and Keasling, J. D. (2008) Trends Biotechnol. 26, 375-381
3. Verdier-Pinard, P., Lai, J. Y., Yoo, H. D., Yu, J., Marquez, B., Nagle, D. G., Nambu, M., White, J. D., Falck, J. R., Gerwick, W. H., Day, B. W., and Hamel, E. (1998) Mol. Pharmacol. 53, 62-76
4. Chang, Z., Sitachitta, N., Rossi, J. V., Roberts, M. A., Flatt, P. M., Jia, J., Sherman, D. H., and Gerwick, W. H. (2004) J. Nat. Prod. 67, 1356-1367
5. Gu, L., Geders, T. W., Wang, B., Gerwick, W. H., Håkansson, K., Smith, J. L., and Sherman, D. H. (2007) Science 318, 970-974
6. Geders, T. W., Gu, L., Mowers, J. C., Liu, H., Gerwick, W. H., Håkansson, K., Sherman, D. H., and Smith, J. L. (2007) J. Biol. Chem. 282, 35954-35963
7. Akey, D. L., Razelun, J. R., Tehranisa, J., Sherman, D. H., Gerwick, W. H., and Smith, J. L. (2010) Structure 18, 94-105
8. Gu, L., Wang, B., Kulkarni, A., Geders, T. W., Grindberg, R. V., Gerwick, L., Håkansson, K., Wipf, P., Smith, J. L., Gerwick, W. H., and Sherman, D. H. (2009) Nature 459, 731-735
9. Gu, L., Wang, B., Kulkarni, A., Gehret, J. J., Lloyd, K. R., Gerwick, L., Gerwick, W. H., Wipf, P., Håkansson, K., Smith, J. L., and Sherman, D. H. (2009) J. Am. Chem. Soc. 131, 16033-16035
10. Chapman, E., Best, M. D., Hanson, S. R., and Wong, C. H. (2004) Angew. Chem. Int. Ed. Engl. 43, 3526-3548
11. Roongsawang, N., Washio, K., and Morikawa, M. (2007) Chembiochem 8, 501-512
12. Giraldes, J. W., Akey, D. L., Kittendorf, J. D., Sherman, D. H., Smith, J. L., and Fecik, R. A. (2006) Nat. Chem. Biol. 2, 531-536
13. Akey, D. L., Kittendorf, J. D., Giraldes, J. W., Fecik, R. A., Sherman, D. H., and Smith, J. L. (2006) Nat. Chem. Biol. 2, 537-542
14. Tsai, S. C., Miercke, L. J., Krucinski, J., Gokhale, R., Chen, J. C., Foster, P. G., Cane, D. E., Khosla, C., and Stroud, R. M. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 14808-14813
15. Scaglione, J. B., Akey, D. L., Sullivan, R., Kittendorf, J. D., Rath, C. M., Kim, E. S., Smith, J. L., and Sherman, D. H. (2010) Angew. Chem. Int. Ed. Engl. 49, 5726-5730
16. Bruner, S. D., Weber, T., Kohli, R. M., Schwarzer, D., Marahiel, M. A., Walsh, C. T., and Stubbs, M. T. (2002) Structure 10, 301-310
17. Samel, S. A., Wagner, B., Marahiel, M. A., and Essen, L. O. (2006) J. Mol. Biol. 359, 876-889
18. Koglin, A., Löhr, F., Bernhard, F., Rogov, V. V., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A., and Dötsch, V. (2008) Nature 454, 907-911
19. Frueh, D. P., Arthanari, H., Koglin, A., Vosburg, D. A., Bennett, A. E., Walsh, C. T., and Wagner, G. (2008) Nature 454, 903-906
20. Claxton, H. B., Akey, D. L., Silver, M. K., Admiraal, S. J., and Smith, J. L. (2009) J. Biol. Chem. 284, 5021-5029
21. DelProposto, J., Majmudar, C. Y., Smith, J. L., and Brown, W. C. (2009) Protein Expr. Purif. 63, 40-49
22. Fischetti, R. F., Xu, S., Yoder, D. W., Becker, M., Nagarajan, V., Sanishvili, R., Hilgart, M. C., Stepanov, S., Makarov, O., and Smith, J. L. (2009) J. Synchrotron Radiat. 16, 217-225
23. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
24. Zwart, P. H., Afonine, P. V., Grosse-Kunstleve, R. W., Hung, L. W., Ioerger, T. R., McCoy, A. J., McKee, E., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., Storoni, L. C., Terwilliger, T. C., and Adams, P. D. (2008) Methods Mol. Biol. 426, 419-435
25. Adams, P. D., Grosse-Kunstleve, R. W., Hung, L. W., Ioerger, T. R., Mc-Coy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., and Terwilliger, T. C. (2002) Acta Crystallogr. D Biol. Crystallogr 58, 1948-1954
26. Terwilliger, T. C. (2000) Acta Crystallogr. D Biol. Crystallogr. 56, 965-972
27. Terwilliger, T. C. (2003) Acta Crystallogr. D Biol. Crystallogr. 59, 38-44
28. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
29. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. D Biol. Crystallogr. 53, 240-255
30. Collaborative Computational Project Number 4 (1994) Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
31. Painter, J., and Merritt, E. A. (2006) Acta Crystallogr. D Biol. Crystallogr. 62, 439-450
32. Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J. (1990) J. Mol. Biol. 215, 403-410
33. Edgar, R. C. (2004) BMC Bioinformatics 5, 113
34. DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific, Palo Alto, CA
35. Schüttelkopf, A. W., and van Aalten, D. M. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 1355-1363
36. Sánchez, C., Du, L., Edwards, D. J., Toney, M. D., and Shen, B. (2001) Chem. Biol. 8, 725-738
37. Gerwick, W. H., Proteau, P. J., Nagle, D. G., Hamel, E., Blokhin, A., and Slate, D. L. (1994) J. Org. Chem. 59, 1243-1245
38. Schirmer, A., Rude, M. A., Li, X., Popova, E., and del Cardayre, S. B. (2010) Science 329, 559-562
39. Steen, E. J., Kang, Y., Bokinsky, G., Hu, Z., Schirmer, A., McClure, A., Del Cardayre, S. B., and Keasling, J. D. (2010) Nature 463, 559-562
40. Metzger, P., and Largeau, C. (2005) Appl. Microbiol. Biotechnol. 66, 486-496
41. Chan Young, T., Largeau, C., and Casadevall, E. (1986) New J. Chem. 10, 701-707
42. Gouet, P., Courcelle, E., Stuart, D. I., and Métoz, F. (1999) Bioinformatics 15, 305-308