Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 65, Issue 12, 2009, Pages 1222-1226

  Padmanabhan, Balasundaram ^a,f   Strange, Richard W ^b   Antonyuk, Svetlana V ^b   Ellis, Mark J ^c   Hasnain, S Samar ^b   Iino, Hitoshi ^d   Agari, Yoshihiro ^d   Bessho, Yoshitaka ^a,d   Yokoyama, Shigeyuki ^a,e  

^a RIKEN YOKOHAMA INSTITUTE   (Japan)

^b UNIVERSITY OF LIVERPOOL   (United Kingdom)

^c DARESBURY LABORATORY   (United Kingdom)

^d Harima Institute ^*  (Japan)

^e UNIVERSITY OF TOKYO   (Japan)

^f Aptuit Laurus Private Limited   (India)

Author keywords

Dihydrodipicolinate synthase; Methanocaldococcus jannaschii

Indexed keywords

DIHYDRODIPICOLINATE SYNTHASE; HYDROLYASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARCHAEAL GENE; ARTICLE; BACILLUS ANTHRACIS; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYME ACTIVE SITE; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METHANOCOCCALES; MOLECULAR CLONING; MOLECULAR GENETICS; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACILLUS ANTHRACIS; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GENES, ARCHAEAL; HYDRO-LYASES; METHANOCOCCALES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN;

BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; METHANOCALDOCOCCUS JANNASCHII; THERMOTOGA MARITIMA;

EID: 74549204509     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S174430910904651X     Document Type: Article

References (22)

1. Blagova, E., Levdikov, V., Milioti, N., Fogg,M. J., Kallioman, A. K., Brannigan, J. A., Wilson, K. S. & Wilkinson, A. J. (2006). Proteins, 62, 297-301.
2. Blickling, S., Renner, C., Laber, B., Pohlenz, H.-D., Holak, T. A. & Huber, R. (1997). Biochemistry, 36, 24-33.
3. 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.
4. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
5. Coulter, C. V., Gerrard, J. A., Kraunsoe, J. A. E. & Pratt, A. J. (1999). Pestic. Sci. 55, 887-895.
6. Cox, R. J., Sutherland, A. & Vederas, J. C. (2000). Bioorg. Med. Chem. 8, 843-871.
7. Cummins, C. S. & Harris, H. (1956). J. Gen. Microbiol. 14, 583-600.
8. DeLano, W. L. (2002). PyMOL Molecular Viewer. DeLano Scientific, San Carlos, California, USA. http://www.pymol.org.
9. Dobson, R. C. J., Gerrard, J. A. & Pearce, F. G. (2004). Biochem. J. 377, 757-762.
10. Dobson, R. C. J., Griffin, M. D. W., Jameson, G. B. & Gerrard, J. A. (2005). Acta Cryst. D61, 1116-1124.
11. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
12. Gouet, P., Courcelle, E., Stuart, D. I. & Mé toz, F. (1999). Bioinformatics, 15, 305-308.
13. Holm, L. & Sander, C. (1993). J. Mol. Biol. 233, 123-138.
14. Hutton, C. A., Southwood, T. J. & Turner, J. J. (2003). Mini Rev. Med. Chem. 3, 115-127.
15. Laskowski, R. A., Moss, D. S. & Thornton, J. M. (1993). J. Mol. Biol. 231, 1049-1067.
16. Mirwaldt, C., Korndorfer, I. & Huber, R. (1995). J. Mol. Biol. 246, 227-239.
17. Morris, R. J., Perrakis, A. & Lamzin, V. S. (2003). Methods Enzymol. 374, 229-244.
18. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Acta Cryst. D53, 240-255.
19. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
20. Pearce, F. G., Perugini, M. A., McKerchar, H. J. & Gerrard, J. A. (2006). Biochem. J. 400, 359-366.
21. Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). Nucleic Acids Res. 22, 4673-4680.
22. Vagin, A. & Teplyakov, A. (1997). J. Appl. Cryst. 30, 1022-1025.