Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 Å Resolution

Journal of Biochemistry

Volumn 127, Issue 3, 2000, Pages 383-391

  Ishii, Noriyuki ^a   Haga, Keiko ^b   Yamane, Kunio ^b   Harata, Kazuaki ^a  

^a NATL INST BIOSCI HUM TECHNOL   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

Acarbose; CGTase; Crystal structure; Cyclodextrin glucanotransferase; X ray crystallography

Indexed keywords

ACARBOSE; ALPHA CYCLODEXTRIN; BETA CYCLODEXTRIN; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; GAMMA CYCLODEXTRIN; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; MOLECULAR MODEL; STRUCTURE ANALYSIS;

BACILLUS; BACILLUS SP.; BACILLUS SP. 1011; BACTERIA (MICROORGANISMS);

EID: 0034027311     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022619     Document Type: Article

References (31)

1. French, D. (1957) The schardinger dextrins. Adv. Carbohydr. Chem. 12, 189-260
2. Schmid, G. (1989) Cyclodextrin glycosyltransferase production: yield enhancement by overexpression of cloned genes. Trends Biotechnol. 7, 224-248
3. Szjitli, S. (1982) Cyclodextrins and Their Inclusion Complexes, Acadmiai Kiad, Budapest
4. Nitschke, L., Heeger, K., Bender, H., and Schulz, G.E. (1990) Molecular cloning, nucleotide sequence and expression in Escherichia coli of the β-cyclodextrin glycosyltransferase gene from Bacillus circulans strain no. 8. Appl. Microbiol. Biotechnol. 33, 542-546
5. Bovetto, L.J., Backer, D.P., Villette, J.R., Sicard, P.J., and Bouquelet, S.J.-L. (1992) Cyclomaltodextrin glucanotransferase from Bacillus circulons E 192, I. Purification and characterization of the enzyme. Biotechnol. Appl. Biochem. 15, 48-58
6. Lawson, C.L., van Montfort, R., Strokopytov, B., Rozeboom, H.J., Kalk, K.H., deVries, G.E., Penninga, D., Dijkhuizen, L., and Dijkstra, B.W. (1994) Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulons strain 251 in a maltose-dependent crystal form. J. Mol. Biol. 236, 590-600
7. Kubota, M., Matsuura, Y., Sakai, S., and Katsube, Y. (1991) Molecular structure of B. stearothermophilus cyclodextrin glucanotransferase and analysis of substrate binding site. Denpun Kagaku 38, 141-146
8. Tanaka, M., Muto, N., and Yamamoto, I. (1991) Characterization of Bacillus stearothermophilus cyclodextrin glucanotransferase in ascorbic acid 2-O-α-glucoside formation. Biochim. Biophys. Acta 1078, 127-132
9. Abe, S., Nagamine, Y., Omichi, K., and Ikenaka, T. (1991) Investigation of the active site of Bacillus macerans cyclodextrin glucanotransferase by use of modified maltooligosaccharides. J. Biochem. 110, 756-761
10. Tomita, K., Kaneda, M., Kawamura, K., and Nakanishi, K. (1993) Purification and properties of a cyclodextrin glucanotransferase from Bacillus autolyticus 11149 and selective formation of β-cyclodextrin. J. Ferment. Bioeng. 75, 89-92
11. Nakamura, A., Haga, K., Ogawa, S., Kuwano, K., Kimura, K., and Yamane, K. (1992) Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α-amylases. FEBS Lett. 296, 37-40
12. Nakamura, A., Haga, K., and Yamane, K. (1993) Three histidine residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: Effects of the replacement on pH dependence and transition-state stabilization. Biochemistry 32, 6624-6631
13. Nakamura, A., Haga, K., and Yamane, K. (1994) The transglycosylation reaction of cyclodextrin glucanotransferase is operated by ping-pong mechanism. FEBS Lett. 337, 66-70
14. Knegtel, R.M.A., Wind, R.D., Rozeboom, H.J., Kalk, K.H., Buitelaar, R.M., Dijkhuizen, L., and Dijkstra, B.W. (1996) Crystal structure at 2.3 Å resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. J. Mol. Biol. 256, 611-622
15. Wind, R.D., Uitdehaag, J.C.M., Buitelaar, R.M., Dijkstra, B.W., and Dijkhuizen, L. (1998) Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. J. Biol. Chem. 273, 5771-5779
16. Szjitli, S. (1988) Cyclodextrin Technology, Kluwer Acad. Publ., Dordrecht
17. Kubota, M., Matsuura, Y., Sakai, S., and Katsube, Y. (1994) Three-dimensional structure of cyclodextrin glucanotransferase and its reaction mechanism. Oyo Toshitsu Kagaku (J. Appl. Glycosci.) 41, 245-253
18. Klein, C. and Schulz, G.E. (1991) Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution. J. Mol. Biol. 217, 737-750
19. Klein, C., Hollender, J., Bender, H., and Schulz, E. (1992) Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis. Biochemistry 31, 8740-8746
20. Knegtel, R.M.A., Strokopytov, B., Penninga, D., Faber, O.G., Rozeboom, H.J., Kalk, K.H., Dijkhuizen, L., and Dijkstra, B.W. (1995) Crystallographic studies of interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products. J. Biol. Chem. 270, 29256-29264
21. Haga, K., Harata, K., Nakamura, A., and Yamane, K. (1994) Crystallization and preliminary X-ray studies of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. J. Mol. Biol. 237, 163-164
22. Harata, K., Haga, K., Nakamura, M., Aoyagi, M., and Yamane, K. (1996) X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. Comparison of two independent molecules at 1.8 Å resolution. Acta Cryst. D52, 1136-1145
23. Strokopytov, B., Penninga, D., Rozeboom, H.J., Kalk, K.H., Dijkhuizen, L., and Dijkstra, B.W. (1995) X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases. Biochemistry 34, 2234-2240
24. Schmidt, A.K., Cottaz, S., Driguez, H., and Schulz, G.E. (1998) Structure of cyclodextrin glucanotransferase complexed with a derivative of its main product β-CD. Biochemistry 37, 5909-5915
25. Strokopytov, B., Knegtel, R.M.A., Penninga, D., Rozeboom, H.J., Kalk, K.H., Dijkhuizen, L., and Dijkstra, B.W. (1996) Structure of cyclodextrin glucanotransferase complexed with maltononaose inhibitor at 2.6 Å resolution. Implication for product specificity. Biochemistry 35, 4241-4249
26. Brunger, A.T., Kuriyan, J., and Karplus, M. (1987) Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460
27. Luzzati, V. (1952) Traitement statistique des erreurs dans la determination des structures cristallines. Acta Cryst. 5, 802-810
28. Ramakrishnan, C. and Ramachandran, G.N. (1965) Stereochemical criteria or polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units. Biophys. J. 5, 909-933
29. Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291
30. Ishii, N., Haga, K., Yamane, K., Harata, K. (2000) Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic Bacillus sp. #1011 determined at 1.9 Å resolution. J. Mol. Recog., in press
31. Mosi, R., Sham, H., Uitdehaag, J.C.M., Ruiterkamp, R., Dijkstra, B.W., and Withers, S.G. (1998) Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase. Biochemistry 37, 17192-17198