Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-β-semialdehyde dehydrogenase

Acta Crystallographica Section D: Biological Crystallography

Volumn 60, Issue 12 II, 2004, Pages 2320-2327

  Faehnle, Christopher R ^a   Blanco, Julio ^a   Viola, Ronald E ^a  

^a UNIVERSITY OF TOLEDO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANION; ARSENIC ACID DERIVATIVE; ASPARTATE SEMIALDEHYDE DEHYDROGENASE; GLUTAMIC ACID; ION; LIGAND; OXYGEN; PERIODATE; PERIODIC ACID; THREONINE;

ARTICLE; BINDING COMPETITION; BINDING SITE; CATALYSIS; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; HAEMOPHILUS INFLUENZAE; HYDROGEN BOND; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION;

ANIONS; ARSENATES; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; BINDING SITES; BINDING, COMPETITIVE; CATALYSIS; GLUTAMIC ACID; HAEMOPHILUS INFLUENZAE; HYDROGEN BONDING; IONS; LIGANDS; MODELS, CHEMICAL; MODELS, MOLECULAR; OXYGEN; PERIODIC ACID; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; THREONINE;

EID: 21644487218     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444904026411     Document Type: Article

References (18)

1. Brandenberger, R., Kammerer, R. A., Engel, J. & Chiquet, M. (1996). J. Cell Biol. 135, 1583-1592.
2. 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.
3. Dutta, S., Akey, I. V., Dingwall, C., Hartman, K. L., Laue, T., Nolte, R. T., Head, J. F. & Akey, C. W. (2001). Mol. Cell, 8, 841-853.
4. Hingorani, K., Szebeni, A. & Olson, M. O. (2000). J. Biol. Chem. 275, 24451-24457.
5. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Cryst. A47, 110-119.
6. Kissinger, C. R., Gehlhaar, D. K. & Fogel, D. B. (1999). Acta Cryst. D55, 484-491.
7. Laskey, R. A., Honda, B. M., Mills, A. D. & Finch, J. T. (1978). Nature (London), 275, 416-420.
8. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
9. Namboodiri, H. V. M., Dutta, S., Akey, I. V., Head, J. F. & Akey, C. W. (2003). Structure, 11, 175-186.
10. Okuwaki, M., Iwamatsu, A., Tsujimoto, M. & Nagata, K. (2001a). J. Mol. Biol. 311, 41-55.
11. Okuwaki, M., Iwamatsu, A., Tsujimoto, M. & Nagata, K. (2001b). FEBS Lett. 506, 272-276.
12. Okuwaki, M., Tsujimoto, M. & Nagata, K. (2002). Mol. Biol. Cell, 13, 2016-2030.
13. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
14. Peculis, B. A. & Gall, J. G. (1992). J. Cell Biol. 116, 1-14.
15. Schmidt-Zachmann, M. S., Hugle-Dorr, B. & Franke, W. W. (1987). EMBO J. 6, 1881-1890.
16. Wang, D., Baumann, A., Szebeni, A. & Olson, M. O. (1994). J. Biol. Chem. 269, 30994-30998.
17. Warner, A. K. & Sloboda, R. D. (1999). Cell Motil. Cytoskeleton, 44, 68-80.
18. Zirwes, R. F., Kouzmenko, A. P., Peters, J. M., Franke, W. W. & Schmidt-Zachmann, M. S. (1997). Mol. Biol. Cell, 8, 231-248.