Structure of aspartate-β-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis

Journal of Molecular Biology

Volumn 289, Issue 4, 1999, Pages 991-1002

  Hadfield, Andrea ^a,b   Kryger, Gitay ^a   Ouyang, Jun ^c   Petsko, Gregory A ^a   Ringe, Dagmar ^a   Viola, Ron ^c  

^a BRANDEIS UNIVERSITY   (United States)

^b UNIVERSITY OF BRISTOL   (United Kingdom)

^c UNIVERSITY OF AKRON   (United States)

Author keywords

Crystal structure; Dehydrogenase; Enzyme; Escherichia coli; NADP

Indexed keywords

ASPARTATE SEMIALDEHYDE DEHYDROGENASE; ASPARTIC ACID; BACTERIAL ENZYME; CYSTEINE; HISTIDINE;

AMINO ACID SYNTHESIS; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

BACTERIA (MICROORGANISMS); EMBRYOPHYTA; ESCHERICHIA COLI; FUNGI;

EID: 0033047006     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2828     Document Type: Article

References (34)

1. Barton G. J. Alscript - a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
2. Bellamacina C. R. The nicotinamide nucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J. 10:1996;1-13.
3. Biellmann J., Eid P., Hirth C., Jornvall H. Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties. Eur. J. Biochem. 104:1980;53-58.
4. Brünger A. T. The R -free value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992a;472-474.
5. Brünger A. T. X-PLOR, Version 3. 1 Manual: A System for X-ray Crystallography and NMR. 1992b;Yale University Press, New Haven.
6. Cardineau G., Curtiss R. Nucleotide sequence of the asd gene of Streptococcus mutans. J. Biol. Chem. 262:1987;3344-3353.
7. CCP4. The CCP4 suite: programmes for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
8. Cohen G. N. The common pathway to lysine, methionine, and threonine. Herrmann K. M., Somerville R. L. Amino Acids: Biosynthesis and Genetic regulation. 1983;166-171 Addison-Wesley Publishing Company, Reading.
9. Cowtan K. 'dm': an automated procedure for phase improvement by density modification. CCP4-ESF-EACBM Newsletter on Protein Crystallography. 31:1994;34-38.
10. Fersht A. Enzyme Structure and Mechanism. 1985;W. H. Freeman and Company, New York.
11. Galan J. E., Nakayama K., Curtiss R. Cloning and characterization of the asd gene of Salmonella typhimurium. Gene. 94:1990;29-35.
12. Harb O. S., Kwaik Y. A. Identification of the asd gene of Legionella pneumophila. Infect. Immun. 66:1998;1898-1903.
13. Haziza C., Stragier P., Patte J. Nucleotide sequence of the asd gene of Escherichia coli. EMBO J. 1:1982;379-384.
14. Holland M., Westhead E. Purification and characterization of aspartic β-semialdehyde dehydrogenase from yeast and purification of an isozyme of glyceraldehyde-3-phosphate dehydrogenase. Biochemistry. 12:1973;2264-2270.
15. Jones T. A., Zou J.-Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron-density maps. Acta Crystallog. sect. A. 47:1991;110-119.
16. Karsten W., Viola R. Chemical and kinetic mechanisms of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Biochim. Biophys. Acta. 1077:1991;209-219.
17. Karsten W., Viola R. Identification of an essential cysteine in the reaction catalyzed by ASADH from Escherichia coli. Biochim. Biophys. Acta. 1121:1992;234-238.
18. Kleywegt G. J., Jones T. A. Halloween... masks and bones. Proceedings of the CCP4 Study Weekend: From First Map to Final Model. 1994;SERC Daresbury Laboratory, Warrington.
19. Kraulis P. MOLSCRIPT: a programme to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
20. Kryger G., Petsko G., Ouyang J., Viola R. Crystallization and preliminary crystallographic analysis of ASADH from Escherichia coli. J. Mol. Biol. 228:1992;300-301.
21. Laskowski R. A., Macarthur M. W., Moss D. S., Thornton J. M. PROCHECK - a programme to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
22. Livingstone C. D., Barton G. J. Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation. Comp. Appl. Biosci. 9:1993;745-756.
23. Moras D., Olsen K. W., Sabesan M. N., Buehner M., Ford G. C., Rossmann M. G. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from lobster. J. Mol. Biol. 250:1975;277-283.
24. Otwinowski Z. Oscillation data reduction programme. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend: Data collection and Processing. 1993;SERC Daresbury Laboratory, Warrington.
25. Ouyang J., Viola R. Use of structural comparisons to select mutagenic targets in ASADH. Biochemistry. 34:1995;6394-6399.
26. Pisabarro A., Malumbres M., Mateos L. M., Oguiza J. A., Martin J. F. A cluster of three genes (dapA, orf2, and dapB) of Brevibacterium lactofermentum encodes dihydrodipicolinate synthase, dihydrodipicolinate reductase, and a third polypeptide of unknown function. J. Bacteriol. 175:1993;2743-2749.
27. Preiss J., Mazelis M., Greenberg E. Cloning of the ASADH structural gene from Escherichia coli K12. Curr. Microbiol. 7:1982;263-268.
28. Ramachandran G. N., Ramakrishnan C., Sasisekharan V. Stereochemistry of polypeptide chain conformations. J. Mol. Biol. 7:1963;95-99.
29. Read R. J. SIGMAA - improved fourier coefficients using calculated phases. Acta Crystallog. sect. A. 42:1986;140-149.
30. Segal H. L., Boyer P. D. Mechanism of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 204:1953;265.
31. Seydoux F., Bernhard S., Pfenninger O., Payne M., Malhotra O. P. Preparation and active-site specific properties of sturgeon muscle glyceraldehyde-3-phosphate dehydrogenase. Biochemistry. 12:1973;4290-4300.
32. Skarzynski T., Wonacott A. J. Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. J. Mol. Biol. 203:1988;1097-1118.
33. Skarzynski T., Moody P. C. E., Wonacott A. J. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution. J. Mol. Biol. 193:1987;171-187.
34. Thierry J., Moras D., Eid P., Hirth C. Crystallization of E. coli aspartate beta-semialdehyde dehydrogenase. Biochimie. 62:1980;739-740.