Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum

Acta Crystallographica Section D: Biological Crystallography

Volumn 64, Issue 6, 2008, Pages 675-685

  Marienhagen, Jan ^a   Sandalova, Tatyana ^b   Sahm, Hermann ^a   Eggeling, Lothar ^a   Schneider, Gunter ^b  

^a FORSCHUNGSZENTRUM JÜLICH   (Germany)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Corynebacterium glutamicum; Histidinol phosphate aminotransferase; Substrate recognition

Indexed keywords

AMINOTRANSFERASE; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; HISTIDINOLPHOSPHATE AMINOTRANSFERASE; PYRIDOXAL 5 PHOSPHATE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CORYNEBACTERIUM GLUTAMICUM; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HYDROGEN BOND; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; CORYNEBACTERIUM GLUTAMICUM; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PYRIDOXAL PHOSPHATE; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TRANSAMINASES;

CORYNEBACTERIUM GLUTAMICUM; ESCHERICHIA COLI; THERMOTOGA MARITIMA;

EID: 45749147800     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444908009438     Document Type: Article

References (27)

1. Cheong, C. G., Escalante-Semerena, J. C. & Rayment, I. (2002). Biochemistry, 41, 9079-9089.
2. Christen, P. & Metzler, D. E. (1985). Transaminases. New York: John Wiley & Sons.
3. Cohen, S. X., Morris, R. J., Fernandez, F. J., Ben Jelloul, M., Kakaris, M., Parthasarathy, V., Lamzin, V. S., Kleywegt, G. J. & Perrakis, A. (2004). Acta Cryst. D60, 2222-2229.
4. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
5. DeLano, W. L. (2002). The PyMOL Molecular Graphics System. http://www.pymol.org.
6. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
7. Fernandez, F. J., Vega, M. C., Lehmann, F., Sandmeier, E., Gehring, H., Christen, P. & Wilmanns, M. (2004). J. Biol. Chem. 279, 21478-21488.
8. Garrick-Silversmith, L. & Hartman, P. E. (1970). Genetics, 66, 231-244.
9. Goto, M., Miyahara, I., Hayashi, H., Kagamiyama, H. & Hirotsu, K. (2003). Biochemistry, 42, 3725-3733.
10. Grishin, N. V., Phillips, M. A. & Goldsmith, E. J. (1995). Protein Sci. 4, 1291-1304.
11. Gu, W., Zhao, G., Eddy, C. & Jensen, R. A. (1995). J. Bacteriol. 177, 1576-1584.
12. Haruyama, K., Nakai, T., Miyahara, I., Hirotsu, K., Mizuguchi, H., Hayashi, H. & Kagamiyama, H. (2001). Biochemistry, 40, 4633-4644.
13. Hirotsu, K., Goto, M., Okamoto, A. & Miyahara, I. (2005). Chem. Rec. 5, 160-172.
14. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
15. Kawaguchi, S. & Kuramitsu, S. (1998). J. Biol. Chem. 273, 18353-18364.
16. Leuchtenberger, W., Huthmacher, K. & Drauz, K. (2005). Appl. Microbiol. Biotechnol. 69, 1-8.
17. Malashkevich, V. N., Onuffer, J. J., Kirsch, J. F. & Jansonius, J. N. (1995). Nature Struct. Biol. 2, 548-553.
18. Marienhagen, J., Kennerknecht, N., Sahm, H. & Eggeling, L. (2005). J. Bacteriol. 187, 7639-7646.
19. Matsui, I., Matsui, E., Sakai, Y., Kikuchi, H., Kawarabayasi, Y., Ura, H., Kawaguchi, S., Kuramitsu, S. & Harata, K. (2000). J. Biol. Chem. 275, 4871-4879.
20. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Acta Cryst. D53, 240-255.
21. Okamoto, A., Nakai, Y., Hayashi, H., Hirotsu, K. & Kagamiyama, H. (1998). J. Mol. Biol. 280, 443-461.
22. Oue, S., Okamoto, A., Nakai, Y., Nakahira, M., Shibatani, T., Hayashi, H. & Kagamiyama, H. (1997). J. Biochem. (Tokyo), 121, 161-171.
23. Schneider, G., Käck, H. & Lindqvist, Y. (2000). Structure, 8, 1-6.
24. Schwarzenbacher, R. et al. (2004). Proteins, 55, 759-763.
25. Sivaraman, J., Li, Y., Larocque, R., Schrag, J. D., Cygler, M. & Matte, A. (2001). J. Mol. Biol. 311, 761-776.
26. Vagin, A. & Teplyakov, A. (1997). J. Appl. Cryst. 30, 1022-1025.
27. Weigent, D. A. & Nester, E. W. (1976). J. Biol. Chem. 251, 6974-6980.