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Volumn 1696, Issue 1, 2004, Pages 103-111

Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin

Author keywords

Allosamidin; Chitinase; Inhibitor; Mutagenesis; Serratia marcescens

Indexed keywords

ALLOSAMIDIN; ASPARAGINE; ASPARTIC ACID; CHITINASE; GLUTAMIC ACID; TRISACCHARIDE; TYROSINE;

EID: 1242284170     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.09.014     Document Type: Article
Times cited : (60)

References (32)
  • 1
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B., Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:1997;637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 2
    • 0032557232 scopus 로고    scopus 로고
    • Substrate distortion to a boat conformation at subsite -1 is critical in the mechanism of family 18 chitinases
    • Brameld K.A., Goddard W.A. Substrate distortion to a boat conformation at subsite -1 is critical in the mechanism of family 18 chitinases. J. Am. Chem. Soc. 120:1998;3571-3580.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3571-3580
    • Brameld, K.A.1    Goddard, W.A.2
  • 3
    • 0032584768 scopus 로고    scopus 로고
    • Substrate assistance in the mechanism of family 18 chitinases: Theoretical studies of potential intermediates and inhibitors
    • Brameld K.A., Shrader W.D., Imperiali B., Goddard W.A. Substrate assistance in the mechanism of family 18 chitinases: theoretical studies of potential intermediates and inhibitors. J. Mol. Biol. 280:1998;913-923.
    • (1998) J. Mol. Biol. , vol.280 , pp. 913-923
    • Brameld, K.A.1    Shrader, W.D.2    Imperiali, B.3    Goddard, W.A.4
  • 5
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis
    • Terwisscha van Scheltinga A.C., Armand S., Kalk K.H., Isogai A., Henrissat B., Dijkstra B.W. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry. 34:1995;15619-15623.
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 7
    • 0029884662 scopus 로고    scopus 로고
    • Comparative studies of chitinases a and B from Serratia marcescens
    • Brurberg M.B., Nes I.F., Eijsink V.G.H. Comparative studies of chitinases A and B from Serratia marcescens. Microbiology. 142:1996;1581-1589.
    • (1996) Microbiology , vol.142 , pp. 1581-1589
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.H.3
  • 9
    • 0035971079 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase
    • Mark B.L., Vocadlo D.J., Knapp S., Triggs-Raine B.L., Withers S.G., James M.N. Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase. J. Biol. Chem. 276:2001;10330-10337.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10330-10337
    • Mark, B.L.1    Vocadlo, D.J.2    Knapp, S.3    Triggs-Raine, B.L.4    Withers, S.G.5    James, M.N.6
  • 10
    • 0037131312 scopus 로고    scopus 로고
    • Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state
    • Williams S.J., Mark B., Vocadlo D.J., James M.N., Withers S.G. Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. J. Biol. Chem. 277:2002;40055-40065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40055-40065
    • Williams, S.J.1    Mark, B.2    Vocadlo, D.J.3    James, M.N.4    Withers, S.G.5
  • 11
    • 0036297773 scopus 로고    scopus 로고
    • The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism
    • Bortone K., Monzingo A.F., Ernst S., Robertus J.D. The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism. J. Mol. Biol. 320:2002;293-302.
    • (2002) J. Mol. Biol. , vol.320 , pp. 293-302
    • Bortone, K.1    Monzingo, A.F.2    Ernst, S.3    Robertus, J.D.4
  • 12
    • 0035949643 scopus 로고    scopus 로고
    • High resolution structural analyses of mutant chitinase a complexes with substrates provide new insight into the mechanism of catalysis
    • Papanikolau Y., Prag G., Tavlas G., Vorgias C.E., Oppenheim A.B., Petratos K. High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry. 40:2001;11338-11343.
    • (2001) Biochemistry , vol.40 , pp. 11338-11343
    • Papanikolau, Y.1    Prag, G.2    Tavlas, G.3    Vorgias, C.E.4    Oppenheim, A.B.5    Petratos, K.6
  • 13
    • 0037321566 scopus 로고    scopus 로고
    • De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase a and its complex with the inhibitor allosamidin
    • Papanikolau Y., Tavlas G., Vorgias C.E., Petratos K. De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin. Acta Crystallogr. 59:2003;400-403.
    • (2003) Acta Crystallogr. , vol.59 , pp. 400-403
    • Papanikolau, Y.1    Tavlas, G.2    Vorgias, C.E.3    Petratos, K.4
  • 14
    • 0036186885 scopus 로고    scopus 로고
    • Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis
    • Bokma E., Rozeboom H.J., Sibbald M., Dijkstra B.W., Beintema J.J. Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis. Eur. J. Biochem. 269:2002;893-901.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 893-901
    • Bokma, E.1    Rozeboom, H.J.2    Sibbald, M.3    Dijkstra, B.W.4    Beintema, J.J.5
  • 15
    • 0028145771 scopus 로고
    • The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation
    • Watanabe T., Ito Y., Yamada T., Hashimoto M., Sekine S., Tanaka H. The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 176:1994;4465-4472.
    • (1994) J. Bacteriol. , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6
  • 16
    • 0023110718 scopus 로고
    • Search for microbial insect growth regulators: II. Allosamidin, a novel insect chitinase inhibitor
    • Sakuda S., Isogai A., Matsumoto S., Suzuki A. Search for microbial insect growth regulators: II. Allosamidin, a novel insect chitinase inhibitor. J. Antibiot. (Tokyo). 40:1987;296-300.
    • (1987) J. Antibiot. (Tokyo) , vol.40 , pp. 296-300
    • Sakuda, S.1    Isogai, A.2    Matsumoto, S.3    Suzuki, A.4
  • 17
    • 0037490208 scopus 로고    scopus 로고
    • Crystal structures of allosamidin derivatives in complex with human macrophage chitinase
    • Rao F.V., Houston D.R., Boot R.G., Aerts J.M., Sakuda S., van Aalten D.M.F. Crystal structures of allosamidin derivatives in complex with human macrophage chitinase. J. Biol. Chem. 278:2003;20110-20116.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20110-20116
    • Rao, F.V.1    Houston, D.R.2    Boot, R.G.3    Aerts, J.M.4    Sakuda, S.5    Van Aalten, D.M.F.6
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 0036008531 scopus 로고    scopus 로고
    • Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 a resolution
    • Kolstad G., Synstad B., Eijsink V.G.H., van Aalten D.M.F. Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution. Acta Crystallogr. 58:2002;377-379.
    • (2002) Acta Crystallogr. , vol.58 , pp. 377-379
    • Kolstad, G.1    Synstad, B.2    Eijsink, V.G.H.3    Van Aalten, D.M.F.4
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. 47:1991;110-119.
    • (1991) Acta Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 22
    • 0030158429 scopus 로고    scopus 로고
    • PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules
    • van Aalten D.M.F., Bywater R., Findlay J.B., Hendlich M., Hooft R.W., Vriend G. PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J. Comput. Aided Mol. Des. 10:1996;255-262.
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 255-262
    • Van Aalten, D.M.F.1    Bywater, R.2    Findlay, J.B.3    Hendlich, M.4    Hooft, R.W.5    Vriend, G.6
  • 23
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 24
    • 0030442990 scopus 로고    scopus 로고
    • Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures
    • Hooft R.W., Sander C., Vriend G. Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. Proteins. 26:1996;363-376.
    • (1996) Proteins , vol.26 , pp. 363-376
    • Hooft, R.W.1    Sander, C.2    Vriend, G.3
  • 25
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta. Crystallogr., A. 32:1976;922-923.
    • (1976) Acta. Crystallogr., a , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D. 50:1994;760-763.
    • (1994) Acta Crystallogr., D , vol.50 , pp. 760-763
  • 27
    • 0037113166 scopus 로고    scopus 로고
    • The cyclic dipeptide CI-4 [cyclo-(L-Arg-D-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediate
    • Houston D.R., Eggleston I., Synstad B., Eijsink V.G.H., van Aalten D.M.F. The cyclic dipeptide CI-4 [cyclo-(L-Arg-D-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediate. Biochem. J. 368:2002;23-27.
    • (2002) Biochem. J. , vol.368 , pp. 23-27
    • Houston, D.R.1    Eggleston, I.2    Synstad, B.3    Eijsink, V.G.H.4    Van Aalten, D.M.F.5
  • 30
    • 0036837290 scopus 로고    scopus 로고
    • Site-directed mutagenesis and functional analysis of active site acidic amino acid residues D142, D144 and E146 in Manduca sexta (tobacco hornworm) chitinase
    • Lu Y., Zen K.C., Muthukrishnan S., Kramer K.J. Site-directed mutagenesis and functional analysis of active site acidic amino acid residues D142, D144 and E146 in Manduca sexta (tobacco hornworm) chitinase. Insect Biochem. Mol. Biol. 32:2002;1369-1382.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1369-1382
    • Lu, Y.1    Zen, K.C.2    Muthukrishnan, S.3    Kramer, K.J.4
  • 31
    • 0028713479 scopus 로고
    • Site-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12
    • Watanabe T., Uchida M., Kobori K., Tanaka H. Site-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12. Biosci. Biotechnol. Biochem. 58:1994;2283-2285.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 2283-2285
    • Watanabe, T.1    Uchida, M.2    Kobori, K.3    Tanaka, H.4
  • 32
    • 1242301196 scopus 로고
    • Zur Konfiguration Stickstoffhaltiger Verbindungen: 13. Uber Die Darstellung und Tautomerie der Aminooxazoline
    • Pitha J., Jonas J., Kovar J., Blaha K. Zur Konfiguration Stickstoffhaltiger Verbindungen: 13. Uber Die Darstellung Und Tautomerie Der Aminooxazoline. Collection of Czechoslovak Chemical Communications. 26:1961;834-846.
    • (1961) Collection of Czechoslovak Chemical Communications , vol.26 , pp. 834-846
    • Pitha, J.1    Jonas, J.2    Kovar, J.3    Blaha, K.4


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