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Volumn 281, Issue 5, 1998, Pages 885-897

Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution

Author keywords

( )8 barrel; Calcium binding; Crystal structure; Isoamylase; Pseudomonas amyloderamosa

Indexed keywords

AMMONIUM SULFATE; CALCIUM ION; ISOAMYLASE;

EID: 0032483304     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1992     Document Type: Article
Times cited : (132)

References (44)
  • 1
    • 0023897655 scopus 로고
    • Cloning and nucleotide sequence of the the isoamylase gene from Pseudomonas amyloderamosa SB-15
    • Amemura A., Chakraborty R., Fujita M., Noumi T., Futai M. Cloning and nucleotide sequence of the the isoamylase gene from Pseudomonas amyloderamosa SB-15. J. Biol. Chem. 263:1988;9271-9275
    • (1988) J. Biol. Chem. , vol.263 , pp. 9271-9275
    • Amemura, A.1    Chakraborty, R.2    Fujita, M.3    Noumi, T.4    Futai, M.5
  • 4
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal
    • Brünger A.T. The free R value a novel statistical quantity for assessing the accuracy of crystal. Nature. 355:1992;472-474
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 5
    • 0023140814 scopus 로고
    • Crystallographic R-factor refinement by molecular dynamics
    • Brünger A.T., Kuriyan J., Karplus M. Crystallographic R-factor refinement by molecular dynamics. Science. 235:1987;458-460
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 6
    • 0030760550 scopus 로고    scopus 로고
    • Structure of the Aspergillus oryzaeα-amylase complexed with the inhibitor acarbose at 2.0 Å resolution
    • Brzozowski A.M., Davies G.J. Structure of the Aspergillus oryzaeα-amylase complexed with the inhibitor acarbose at 2.0 Å resolution. Biochemistry. 36:1997;10837-10845
    • (1997) Biochemistry , vol.36 , pp. 10837-10845
    • Brzozowski, A.M.1    Davies, G.J.2
  • 7
    • 0025131206 scopus 로고
    • Nucleotide sequence and expression of the isoamylase gene from an isoamylase-hyperproducing mutant, Pseudomonas amyloderamosa JD210
    • Chen J.H., Chen Z.Y., Chow T.W., Chen J.C., Tan S.T., Hsu W.H. Nucleotide sequence and expression of the isoamylase gene from an isoamylase-hyperproducing mutant, Pseudomonas amyloderamosa JD210. Biochim. Biophys. Acta. 1087:1990;309-315
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 309-315
    • Chen, J.H.1    Chen, Z.Y.2    Chow, T.W.3    Chen, J.C.4    Tan, S.T.5    Hsu, W.H.6
  • 8
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies G.J., Wilson K.S., Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321:1997;557-559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 9
    • 0002701928 scopus 로고
    • PHASES: A program package for the processing and analysis of diffraction data from macromolecules
    • Furey W., Swaminathan S. PHASES a program package for the processing and analysis of diffraction data from macromolecules. Am. Crystallog. Assoc. Annu. Mtg Program Abstr. 18:1990;73
    • (1990) Am. Crystallog. Assoc. Annu. Mtg Program Abstr. , vol.18 , pp. 73
    • Furey, W.1    Swaminathan, S.2
  • 10
    • 0029953633 scopus 로고    scopus 로고
    • Crystal structure of pig pancreatic α-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose
    • Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F. Crystal structure of pig pancreatic α-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose. Eur. J. Biochem. 238:1996;561-569
    • (1996) Eur. J. Biochem. , vol.238 , pp. 561-569
    • Gilles, C.1    Astier, J.-P.2    Marchis-Mouren, G.3    Cambillau, C.4    Payan, F.5
  • 12
    • 0002193613 scopus 로고
    • The processing of diffraction data taken on a screenless Weisenberg camera for macromolecular crystallography
    • Higashi T. The processing of diffraction data taken on a screenless Weisenberg camera for macromolecular crystallography. J. Appl. Crystallog. 22:1989;9-18
    • (1989) J. Appl. Crystallog. , vol.22 , pp. 9-18
    • Higashi, T.1
  • 13
    • 0026040317 scopus 로고
    • Comparison of the domain level organization of starch hydrolases and related enzymes
    • Jespersen H.M., MacGregor E.A., Sierks M.R., Svensson B. Comparison of the domain level organization of starch hydrolases and related enzymes. Biochem. J. 280:1991;51-55
    • (1991) Biochem. J. , vol.280 , pp. 51-55
    • Jespersen, H.M.1    MacGregor, E.A.2    Sierks, M.R.3    Svensson, B.4
  • 15
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical feature
    • Kabsch W., Sander C. Dictionary of protein secondary structure pattern recognition of hydrogen bonded and geometrical feature. Biopolymers. 22:1983;2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 16
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • Kadziola A., Abe J., Svensson B., Haser R. Crystal and molecular structure of barley α-amylase. J. Mol. Biol. 239:1994;104-121
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.2    Svensson, B.3    Haser, R.4
  • 17
    • 0027176843 scopus 로고
    • Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6,-glucosidase revealed by 3.0 Å resolution X-ray analysis
    • Kizaki H., Hata Y., Watanabe Y., Katsube Y., Suzuki Y. Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6,-glucosidase revealed by 3.0 Å resolution X-ray analysis. J. Biochem. (Tokyo). 113:1993;646-649
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 646-649
    • Kizaki, H.1    Hata, Y.2    Watanabe, Y.3    Katsube, Y.4    Suzuki, Y.5
  • 18
    • 0026027728 scopus 로고
    • Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution
    • Klein C., Schulz G.E. Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution. J. Mol. Biol. 217:1991;737-750
    • (1991) J. Mol. Biol. , vol.217 , pp. 737-750
    • Klein, C.1    Schulz, G.E.2
  • 19
    • 0028880402 scopus 로고
    • Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products
    • Knegtel R.M., Strokopytov B., Penninga D., Faber O.G., Rozenboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W. Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products. J. Biol. Chem. 270:1995;29256-29264
    • (1995) J. Biol. Chem. , vol.270 , pp. 29256-29264
    • Knegtel, R.M.1    Strokopytov, B.2    Penninga, D.3    Faber, O.G.4    Rozenboom, H.J.5    Kalk, K.H.6    Dijkhuizen, L.7    Dijkstra, B.W.8
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0001737019 scopus 로고
    • Molecular structure of Bacillus stearothermophilus cyclodextrin glucanotransferase and analysis of the substrate binding site
    • Kubota M., Matsuura Y., Sakai S., Katsube Y. Molecular structure of Bacillus stearothermophilus cyclodextrin glucanotransferase and analysis of the substrate binding site. Denpun Kagaku. 38:1991;141-146
    • (1991) Denpun Kagaku , vol.38 , pp. 141-146
    • Kubota, M.1    Matsuura, Y.2    Sakai, S.3    Katsube, Y.4
  • 22
    • 0024382861 scopus 로고
    • Nucleotide sequence of the neopullulanase gene from Bacillusstearothermophilus
    • Kuriki T., Imanaka T. Nucleotide sequence of the neopullulanase gene from Bacillusstearothermophilus. J. Gen. Microbiol. 135:1989;1521-1528
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1521-1528
    • Kuriki, T.1    Imanaka, T.2
  • 23
    • 0028359337 scopus 로고
    • Refined molecular structure of pig pancreatic α-amylase at 2.1 Å resolution
    • Larson S.B., Greenwood A., Casico D., Day J., Mcpherson A. Refined molecular structure of pig pancreatic α-amylase at 2.1 Å resolution. J. Mol. Biol. 235:1994;1560-1584
    • (1994) J. Mol. Biol. , vol.235 , pp. 1560-1584
    • Larson, S.B.1    Greenwood, A.2    Casico, D.3    Day, J.4    McPherson, A.5
  • 24
    • 0001099937 scopus 로고
    • Traitment statistique des erreures dans la determination des structures cristallines
    • Luzzati P.V. Traitment statistique des erreures dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 25
    • 0024514666 scopus 로고
    • A super-secondary structure predicted to be common to several α-1,4-D-glucan-cleaving enzymes
    • MacGregor E.A., Svensson B. A super-secondary structure predicted to be common to several α-1,4-D-glucan-cleaving enzymes. Biochem. J. 259:1989;145-152
    • (1989) Biochem. J. , vol.259 , pp. 145-152
    • MacGregor, E.A.1    Svensson, B.2
  • 26
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformisα-amylase at 2.2 Å resolution
    • Machius M., Wiegand G., Huber R. Crystal structure of calcium-depleted Bacillus licheniformisα-amylase at 2.2 Å resolution. J. Mol. Biol. 246:1995;545-559
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • MacHius, M.1    Wiegand, G.2    Huber, R.3
  • 27
  • 28
    • 0000278405 scopus 로고
    • Structure and catalytic implication of Taka-amylase a
    • Matsuura Y., Kusunoki M., Kakudo M. Structure and catalytic implication of Taka-amylase A. Denpun Kagaku. 38:1991;137-139
    • (1991) Denpun Kagaku , vol.38 , pp. 137-139
    • Matsuura, Y.1    Kusunoki, M.2    Kakudo, M.3
  • 30
    • 0022670999 scopus 로고
    • Comparison of amino acid sequences of eleven different α-amylases
    • Nakajima R., Imanaka T., Aiba S. Comparison of amino acid sequences of eleven different α-amylases. Appl. Microbiol. Biotechnol. 23:1986;355-360
    • (1986) Appl. Microbiol. Biotechnol. , vol.23 , pp. 355-360
    • Nakajima, R.1    Imanaka, T.2    Aiba, S.3
  • 31
    • 0027296794 scopus 로고
    • Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution
    • Qian M., Haser R., Payan F. Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution. J. Mol. Biol. 231:1993;785-799
    • (1993) J. Mol. Biol. , vol.231 , pp. 785-799
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 32
    • 0028198814 scopus 로고
    • The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution
    • Qian M., Haser R., Buisson G., Duee E., Payan F. The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution. Biochemistry. 33:1994;6284-6294
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 33
    • 0028966756 scopus 로고
    • Carbohydrate binding sites in a pancreatic α-amylase-substrate complex, derived from X-ray structure analysis at 2.1 Å resolution
    • Qian M., Haser R., Payan F. Carbohydrate binding sites in a pancreatic α-amylase-substrate complex, derived from X-ray structure analysis at 2.1 Å resolution. Protein Sci. 4:1995;747-755
    • (1995) Protein Sci. , vol.4 , pp. 747-755
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 34
    • 0001631469 scopus 로고    scopus 로고
    • Structure of human salivary α-amylase at 1.6 Å resolution: Implication for its role in the oral cavity
    • Ramasubbu N., Paloth V., Luo Y., Brayer G.D., Levine M. Structure of human salivary α-amylase at 1.6 Å resolution implication for its role in the oral cavity. Acta Crystallog. sect. D. 52:1996;435-446
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 435-446
    • Ramasubbu, N.1    Paloth, V.2    Luo, Y.3    Brayer, G.D.4    Levine, M.5
  • 35
    • 0000525517 scopus 로고
    • A focusing Weissenberg camera with multi-layer-line screens for macromolecular crystallography
    • Sakabe N. A focusing Weissenberg camera with multi-layer-line screens for macromolecular crystallography. J. Appl. Crystallog. 16:1983;542-545
    • (1983) J. Appl. Crystallog. , vol.16 , pp. 542-545
    • Sakabe, N.1
  • 37
    • 0028961637 scopus 로고
    • X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases
    • Strokopytov B., Penninga D., Rozenboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W. X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases. Biochemistry. 34:1995;2234-2240
    • (1995) Biochemistry , vol.34 , pp. 2234-2240
    • Strokopytov, B.1    Penninga, D.2    Rozenboom, H.J.3    Kalk, K.H.4    Dijkhuizen, L.5    Dijkstra, B.W.6
  • 38
    • 0029931070 scopus 로고    scopus 로고
    • Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity
    • Strokopytov B., Knegtel M.A., Penninga D., Rozenboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W. Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity. Biochemistry. 35:1996;4241-4249
    • (1996) Biochemistry , vol.35 , pp. 4241-4249
    • Strokopytov, B.1    Knegtel, M.A.2    Penninga, D.3    Rozenboom, H.J.4    Kalk, K.H.5    Dijkhuizen, L.6    Dijkstra, B.W.7
  • 39
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity and stability
    • Svensson B. Protein engineering in the α-amylase family catalytic mechanism, substrate specificity and stability. Plant Mol. Biol. 25:1994;141-157
    • (1994) Plant Mol. Biol. , vol.25 , pp. 141-157
    • Svensson, B.1
  • 42
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol. 269:1997;142-153
    • (1997) J. Mol. Biol. , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 43
    • 0025113022 scopus 로고
    • β-Turns and their distortions: A proposed new nomenclature
    • Wilmot C.M., Thornton J.M. β-Turns and their distortions a proposed new nomenclature. Protein Eng. 3:1990;479-493
    • (1990) Protein Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thornton, J.M.2
  • 44
    • 0030823127 scopus 로고    scopus 로고
    • Crystal structure of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose
    • Yoshioka Y., Hasegawa K., Matsuura Y., Katsuabe Y., Kubota M. Crystal structure of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose. J. Mol. Biol. 271:1997;619-628
    • (1997) J. Mol. Biol. , vol.271 , pp. 619-628
    • Yoshioka, Y.1    Hasegawa, K.2    Matsuura, Y.3    Katsuabe, Y.4    Kubota, M.5


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