Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans

Journal of Molecular Biology

Volumn 290, Issue 1, 1999, Pages 161-173

  Cobessi, David ^a   Tête Favier, Frédérique ^a   Marchal, Stéphane ^b   Azza, Saïd ^b   Branlant, Guy ^b   Aubry, André ^a  

^a Nancy University CNRS   (France)

^b Biopôle de l Université de Lorraine   (France)

Author keywords

Aldehyde dehydrogenase; Cofactor specificity; NADP; Substrate specificity; X ray structure

Indexed keywords

ADENOSINE; ALDEHYDE DEHYDROGENASE; GLYCERALDEHYDE 3 PHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ISOLATION; ENZYME STRUCTURE; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; STREPTOCOCCUS MUTANS;

BACTERIA (MICROORGANISMS); POSIBACTERIA; STREPTOCOCCUS MUTANS;

EID: 0033516517     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2853     Document Type: Article

References (29)

1. Bergdoll M., Remy M.-H., Cagnon C., Masson J.-M., Dumas P. Proline dependent oligomerization with arm exchange. Structure. 5:1997;391-401.
2. Boyd D. A., Cvitkovitch D. G., Hamilton I. R. Sequence, expression, and function of the gene for the non phosphorylating, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus mutans. J. Bacteriol. 177:1995;2622-2627.
3. Brünger A. T. X-PLOR Manual. 1990;Yale University Press, New Haven.
4. freevalue: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475.
5. +-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. J. Biol. Chem. 273:1998;6149-6156.
6. +-dependent glyceraldehyde-3-phosphate dehydrogenases from Streptococcus mutans. J. Biol. Chem. 254:1979;1134-1142.
7. Gouet P., Courcelle E., Stuart D., Metoz F. SPript: analysis of multiple sequence alignments in PostScript. Bioinformatics. 15:1999;305-308.
8. Habenicht A., Hellman U., Cerff R. Non-phosphorylating GAPDH of higher plants is a member of the aldehyde dehydrogenase superfamily with no sequence homology with the phosphorylating GAPDH. J. Mol. Biol. 237:1994;165-171.
9. Hol W. G. J. The role of the α-helix dipole in protein function and structure. Prog. Biophys. Mol. Biol. 45:1985;149-195.
10. Johansson K., El-Ahmad M., Ramaswamy S., Hjelmqvist L., Jörnvall H., Eklund H. Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution. Protein Sci. 7:1998;2106-2117.
11. Jones T. A., Kjeldgaard M. "O" Manual, version 6.1. 1990;Uppsala University, Sweden and Aarhus University.
12. Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
13. Kraulis P. J. MOLSCRPIT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
14. Laskowsky R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
15. Liu Z. L., Sun Y.-J., Rose J., Chung Y. J., Hsiao C.-D., Chang W.-R., Kuo I., Perozich J., Lindahl R., Hempel J., Wang B.-C. The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. Nature Struct. Biol. 4:1997;317-326.
16. Meritt E. A., Murphy M. E. P. Raster3D version 2. 4-A program for photo-realistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
17. Moore S. A., Baker H. M., Blythe T. J., Kitson K. E., Kitson T. M., Baker E. N. Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases. Structure. 6:1998;1541-1551.
18. Moras D., Olsen K. W., Sabesan M. N., Buehner M., Ford G. C., Rossmann M. G. Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 250:1975;9137-9162.
19. Navaza J. AMoRe: An automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
20. Otwinowsky Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
21. Rossmann M. G., Moras D., Olsen K. W. Chemical and biological evolution of a nucleotide-binding protein. Nature. 250:1974;194-199.
22. Roussel P. A., Cambillau C. TURBO-FRODO, Silicon Graphics applications directory. 1991;Silicon Graphics, Mountain View.
23. Sali A., Blundell T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
24. Sheikh S., Ni L., Hurley T. D., Weiner H. The potential roles of the conserved amino acids in human liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 272:1997;18817-18822.
25. Sidman K. E., George D. G., Barker W. C., Hunt L. T. The protein identification resource (PIR). Nucl. Acids Res. 16:1998;1869-1871.
26. Skarzynsky 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.
27. Steinmetz C. G., Xie P., Weiner H., Hurley D. T. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure. 5:1997;701-711.
28. ??? December 1996.
29. Yoshida A., Rzhetsky A., Hsu L. C., Chang C. Human aldehyde dehydrogenase gene family. Eur. J. Biochem. 251:1998;549-557.