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Volumn 273, Issue 17, 2006, Pages 3962-3974

cDNA cloning and 1.75 Å crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds

Author keywords

Endochitinase; Glycosyl hydrolase family 18; Mimosoideae; Parkia platycephala; X ray crystal structure

Indexed keywords

CHITIN; CHITINASE; COMPLEMENTARY DNA; ENDOCHITINASE; GENOMIC DNA; GLYCOSIDASE; HEMAGGLUTININ; LECTIN; LECTIN 2; N ACETYLGLUCOSAMINE; RNA; UNCLASSIFIED DRUG;

EID: 33747413686     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05400.x     Document Type: Article
Times cited : (28)

References (52)
  • 1
    • 0032422738 scopus 로고    scopus 로고
    • Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles
    • Van Damme EJM, Peumans WJ, Barre A & Rougé P (1998) Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit Rev Plant Sci 17, 575-692.
    • (1998) Crit Rev Plant Sci , vol.17 , pp. 575-692
    • Van Damme, E.J.M.1    Peumans, W.J.2    Barre, A.3    Rougé, P.4
  • 3
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity
    • Dodd RB & Drickamer K (2001) Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiology 11, 71-79.
    • (2001) Glycobiology , vol.11 , pp. 71-79
    • Dodd, R.B.1    Drickamer, K.2
  • 5
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis WI & Drickamer K (1996) Structural basis of lectin-carbohydrate recognition. Annu Rev Biochem 65, 441-473.
    • (1996) Annu Rev Biochem , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 6
    • 0030666313 scopus 로고    scopus 로고
    • Lectin-carbohydrate interactions: Different folds, common recognition principles
    • Elgavish S & Shaanan B (1997) Lectin-carbohydrate interactions: different folds, common recognition principles. Trends Biochem Sci 22, 462-467.
    • (1997) Trends Biochem Sci , vol.22 , pp. 462-467
    • Elgavish, S.1    Shaanan, B.2
  • 8
    • 0032872116 scopus 로고    scopus 로고
    • Novel structures of plant lectins and their complexes with carbohydrates
    • Bouckaert J, Hamelryck T, Wyns L & Loris R (1999) Novel structures of plant lectins and their complexes with carbohydrates. Curr Opin Struct Biol 9, 572-577.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 572-577
    • Bouckaert, J.1    Hamelryck, T.2    Wyns, L.3    Loris, R.4
  • 10
    • 0029052976 scopus 로고
    • Calorimetric analysis of the binding of lectins with overlapping carbohydrate binding
    • Chervenak MC & Toone EJ (1995) Calorimetric analysis of the binding of lectins with overlapping carbohydrate binding. Biochemistry 34, 5685-5695.
    • (1995) Biochemistry , vol.34 , pp. 5685-5695
    • Chervenak, M.C.1    Toone, E.J.2
  • 11
    • 0032524862 scopus 로고    scopus 로고
    • Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates
    • Dam TK, Cavada BS, Grangeiro TB, Santos CF, de Sousa FAM, Oscarson S & Brewer CF (1998) Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates. J Biol Chem 273, 12082-12088.
    • (1998) J Biol Chem , vol.273 , pp. 12082-12088
    • Dam, T.K.1    Cavada, B.S.2    Grangeiro, T.B.3    Santos, C.F.4    De Sousa, F.A.M.5    Oscarson, S.6    Brewer, C.F.7
  • 12
    • 0034717073 scopus 로고    scopus 로고
    • Thermodynamic binding studies of lectins from the diocleinae subtribe to deoxy analogs of the core trimannoside of asparagine-linked oligosaccharides
    • Dam TK, Cavada BS, Grangeiro TB, Santos CF, Ceccatto VM, de Sousa FAM, Oscarson S & Brewer CF (2000) Thermodynamic binding studies of lectins from the diocleinae subtribe to deoxy analogs of the core trimannoside of asparagine-linked oligosaccharides. J Biol Chem 275, 16119-16126.
    • (2000) J Biol Chem , vol.275 , pp. 16119-16126
    • Dam, T.K.1    Cavada, B.S.2    Grangeiro, T.B.3    Santos, C.F.4    Ceccatto, V.M.5    De Sousa, F.A.M.6    Oscarson, S.7    Brewer, C.F.8
  • 13
    • 0034640419 scopus 로고    scopus 로고
    • Binding of multivalent carbohydrates to concanavalin a and Dioclea grandiflora lectin. Thermodynamic analysis of the 'multivalency effect'
    • Dam TK, Roy R, Das SK, Oscarson S & Brewer CF (2000) Binding of multivalent carbohydrates to concanavalin A and Dioclea grandiflora lectin. Thermodynamic analysis of the 'multivalency effect'. J Biol Chem 275, 14223-14230.
    • (2000) J Biol Chem , vol.275 , pp. 14223-14230
    • Dam, T.K.1    Roy, R.2    Das, S.K.3    Oscarson, S.4    Brewer, C.F.5
  • 15
    • 0029163653 scopus 로고
    • Purification of a lectin from Parkia javanica beans
    • Utarabhand P & Akkayanont P (1995) Purification of a lectin from Parkia javanica beans. Phytochemistry 38, 281-285.
    • (1995) Phytochemistry , vol.38 , pp. 281-285
    • Utarabhand, P.1    Akkayanont, P.2
  • 19
    • 0034818010 scopus 로고    scopus 로고
    • The amino-acid sequence of the glucose/mannose-specific lectin isolated from Parkia platycephala seeds reveals three tandemly arranged jacalin-related domains
    • Mann K, Farias CM, Gallego del Sol FG, Santos CF, Grangeiro TB, Nagano CS, Cavada BS & Calvete JJ (2001) The amino-acid sequence of the glucose/mannose-specific lectin isolated from Parkia platycephala seeds reveals three tandemly arranged jacalin-related domains. Eur J Biochem 268, 4414-4422.
    • (2001) Eur J Biochem , vol.268 , pp. 4414-4422
    • Mann, K.1    Farias, C.M.2    Gallego Del Sol, F.G.3    Santos, C.F.4    Grangeiro, T.B.5    Nagano, C.S.6    Cavada, B.S.7    Calvete, J.J.8
  • 20
    • 26444475342 scopus 로고    scopus 로고
    • Energetics of 5-bromo-4-chloro-3-indolyl-α-D-mannose binding to the Parkia platycephala seed lectin and its use for MAD phasing
    • Gallego del Sol F, Gómez J, Hoos C, Nagano CS, Cavada BS, England P & Calvete JJ (2005) Energetics of 5-bromo-4-chloro-3-indolyl-α-D- mannose binding to the Parkia platycephala seed lectin and its use for MAD phasing. Acta Cryst F 61, 326-331.
    • (2005) Acta Cryst F , vol.61 , pp. 326-331
    • Gallego Del Sol, F.1    Gómez, J.2    Hoos, C.3    Nagano, C.S.4    Cavada, B.S.5    England, P.6    Calvete, J.J.7
  • 21
    • 26444524471 scopus 로고    scopus 로고
    • The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain
    • Gallego del Sol F, Nagano CS, Cavada BS & Calvete JJ (2005) The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain. J Mol Biol 353, 574-583.
    • (2005) J Mol Biol , vol.353 , pp. 574-583
    • Gallego Del Sol, F.1    Nagano, C.S.2    Cavada, B.S.3    Calvete, J.J.4
  • 22
    • 0003657026 scopus 로고
    • Harborne JB & Boulter D, eds, Academic Press, London
    • Heywood VH (1971) Chemotaxonomy of the Leguminosae (Harborne JB & Boulter D, eds), pp. 1-29. Academic Press, London.
    • (1971) Chemotaxonomy of the Leguminosae , pp. 1-29
    • Heywood, V.H.1
  • 23
    • 0025718126 scopus 로고
    • Lectins, lectin genes, and their role in plant defense
    • Chrispeels MJ & Raikhel NV (1991) Lectins, lectin genes, and their role in plant defense. Plant Cell 3, 1-9.
    • (1991) Plant Cell , vol.3 , pp. 1-9
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 24
    • 16344393419 scopus 로고    scopus 로고
    • Characterization of a jasmonate-regulated wheat protein related to a β-glucosidase-aggregating factor
    • Wang X & Ma Q (2005) Characterization of a jasmonate-regulated wheat protein related to a β-glucosidase-aggregating factor. Plant Physiol Biochem 43, 185-192.
    • (2005) Plant Physiol Biochem , vol.43 , pp. 185-192
    • Wang, X.1    Ma, Q.2
  • 26
    • 0030909499 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among chitinases of flowering plants
    • Hamel F, Boivin R, Tremblay C & Bellemare G (1997) Structural and evolutionary relationships among chitinases of flowering plants. J Mol Evol 44, 614-624.
    • (1997) J Mol Evol , vol.44 , pp. 614-624
    • Hamel, F.1    Boivin, R.2    Tremblay, C.3    Bellemare, G.4
  • 27
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases - Regulation and function
    • Kasprzewska A (2003) Plant chitinases - regulation and function. Cell Mol Biol Lett 8, 809-824.
    • (2003) Cell Mol Biol Lett , vol.8 , pp. 809-824
    • Kasprzewska, A.1
  • 29
    • 0027321099 scopus 로고
    • Thyroglobulin glycosylation: Location and nature of the N-linked oligosaccharide units in bovine thyroglobulin
    • Rawitch AB, Pollock HG & Yang S-X (1993) Thyroglobulin glycosylation: location and nature of the N-linked oligosaccharide units in bovine thyroglobulin. Arch Biochem Biophys 300, 271-279.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 271-279
    • Rawitch, A.B.1    Pollock, H.G.2    Yang, S.-X.3
  • 30
    • 0017374109 scopus 로고
    • Purification, composition, molecular weight, and subunit structure of ovine submaxillary mucin
    • Hill HD Jr, Reynolds JA & Hill RL (1977) Purification, composition, molecular weight, and subunit structure of ovine submaxillary mucin. J Biol Chem 252, 3791-3798.
    • (1977) J Biol Chem , vol.252 , pp. 3791-3798
    • Hill Jr., H.D.1    Reynolds, J.A.2    Hill, R.L.3
  • 31
    • 0016245734 scopus 로고
    • Structure of the O-glycosidically linked carbohydrate units of fetuin
    • Spiro RG & Bhoyroo D (1974) Structure of the O-glycosidically linked carbohydrate units of fetuin. J Biol Chem 249, 5704-5717.
    • (1974) J Biol Chem , vol.249 , pp. 5704-5717
    • Spiro, R.G.1    Bhoyroo, D.2
  • 33
    • 0027165850 scopus 로고
    • Identification, quantitation, and characterization of glycopeptides in reversed-phase HPLC separations of glycoprotein proteolytic digests
    • Rohrer JS, Cooper GA & Townsend RR (1993) Identification, quantitation, and characterization of glycopeptides in reversed-phase HPLC separations of glycoprotein proteolytic digests. Anal Biochem 212, 7-16.
    • (1993) Anal Biochem , vol.212 , pp. 7-16
    • Rohrer, J.S.1    Cooper, G.A.2    Townsend, R.R.3
  • 34
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280, 309-316.
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 35
    • 0025739769 scopus 로고
    • The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex
    • Jekel PA, Hartmann BH & Beintema JJ (1991) The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex. Eur J Biochem 200, 123-130.
    • (1991) Eur J Biochem , vol.200 , pp. 123-130
    • Jekel, P.A.1    Hartmann, B.H.2    Beintema, J.J.3
  • 36
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Van Scheltinga ACT, Kalk KH, Beintema JJ & Dijkstra BW (1994) Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 2, 1181-1189.
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Van Scheltinga, A.C.T.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 37
    • 15444365716 scopus 로고    scopus 로고
    • An agglutinating chitinase with two chitin-binding domains confers fungal protection in transgenic potato
    • Chye ML, Zhao KJ, He ZM, Ramalingam S & Fung KL (2005) An agglutinating chitinase with two chitin-binding domains confers fungal protection in transgenic potato. Planta 220, 717-730.
    • (2005) Planta , vol.220 , pp. 717-730
    • Chye, M.L.1    Zhao, K.J.2    He, Z.M.3    Ramalingam, S.4    Fung, K.L.5
  • 39
    • 0033290345 scopus 로고    scopus 로고
    • The structure and action of chitinases
    • Robertus JD & Monzingo AF (1999) The structure and action of chitinases. EXS 87, 125-135.
    • (1999) EXS , vol.87 , pp. 125-135
    • Robertus, J.D.1    Monzingo, A.F.2
  • 40
    • 0041350370 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of an antifungal chitinase from Leucaena leucocephala de Wit
    • Kaomek M, Mizuno K, Fujimura T, Sriyotha P & Cairns JR (2003) Cloning, expression, and characterization of an antifungal chitinase from Leucaena leucocephala de Wit. Biosci Biotechnol Biochem 67, 667-676.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 667-676
    • Kaomek, M.1    Mizuno, K.2    Fujimura, T.3    Sriyotha, P.4    Cairns, J.R.5
  • 41
    • 0028845991 scopus 로고
    • Crystal structure of concanavalin B at 1.65 a resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis
    • Hennig M, Jansonius JN, Van Scheltinga ACT, Dijkstra BW & Schlesier BJ (1995) Crystal structure of concanavalin B at 1.65 A resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis. J Mol Biol 254, 237-246.
    • (1995) J Mol Biol , vol.254 , pp. 237-246
    • Hennig, M.1    Jansonius, J.N.2    Van Scheltinga, A.C.T.3    Dijkstra, B.W.4    Schlesier, B.J.5
  • 42
    • 0030595119 scopus 로고    scopus 로고
    • The 1.8 a ° resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18
    • Van Scheltinga ACT, Hennig M & Dijkstra BW (1996) The 1.8 A ° resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18. J Mol Biol 262, 243-257.
    • (1996) J Mol Biol , vol.262 , pp. 243-257
    • Van Scheltinga, A.C.T.1    Hennig, M.2    Dijkstra, B.W.3
  • 44
    • 0027943884 scopus 로고
    • A structural analysis of phosphate and sulphate binding sites in proteins. Estimation of propensities for binding and conservation of phosphate binding sites
    • Copley RR & Barton GJ (1994) A structural analysis of phosphate and sulphate binding sites in proteins. Estimation of propensities for binding and conservation of phosphate binding sites. J Mol Biol 242, 321-329.
    • (1994) J Mol Biol , vol.242 , pp. 321-329
    • Copley, R.R.1    Barton, G.J.2
  • 45
    • 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 HJ, Sibbald M, Dijkstra BW & Beintema JJ (2002) Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis. Eur J Biochem 269, 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
  • 46
    • 0029808206 scopus 로고    scopus 로고
    • Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation
    • Pastuszak I, Drake R & Elbein AD (1996) Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation. J Biol Chem 271, 20776-20782.
    • (1996) J Biol Chem , vol.271 , pp. 20776-20782
    • Pastuszak, I.1    Drake, R.2    Elbein, A.D.3
  • 48
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H & von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166, 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 49
    • 0021312893 scopus 로고
    • Amino acid analysis by reversed-phase high-performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate
    • Henrikson RL & Meredith SC (1984) Amino acid analysis by reversed-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate. Anal Biochem 136, 65-71.
    • (1984) Anal Biochem , vol.136 , pp. 65-71
    • Henrikson, R.L.1    Meredith, S.C.2
  • 51
    • 0000494289 scopus 로고
    • Rapid amplification of cDNA ends using nested primers
    • Frohman MA & Martin GR (1989) Rapid amplification of cDNA ends using nested primers. Techniques 1, 165-170.
    • (1989) Techniques , vol.1 , pp. 165-170
    • Frohman, M.A.1    Martin, G.R.2
  • 52
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 (1994). Acta Cryst D50, 760-763.
    • (1994) Acta Cryst , vol.D50 , pp. 760-763


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