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Volumn 334, Issue 3, 2003, Pages 421-433

The structural bases of the processive degradation of ι-carrageenan, a main cell wall polysaccharide of red algae

Author keywords

Electron microscopy; Iota carrageenase; Processivity; Sulfated polysaccharide; X ray structure

Indexed keywords

ASPARTIC ACID DERIVATIVE; BACTERIAL ENZYME; CARRAGEENAN; DISACCHARIDE; GLUTAMIC ACID DERIVATIVE; IOTA CARRAGEENASE; POLYSACCHARIDE; PROTON; SULFATE; UNCLASSIFIED DRUG;

EID: 0242579170     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.056     Document Type: Article
Times cited : (57)

References (66)
  • 1
    • 0014140609 scopus 로고
    • Multiple attack hypothesis of α-amylase action: Action of porcine pancreatic, human salivary, and Aspergilus oryzae α-amylases
    • Robyt J.S., French D. Multiple attack hypothesis of α-amylase action: action of porcine pancreatic, human salivary, and Aspergilus oryzae α-amylases. Arch. Biochem. Biophys. 122:1967;8-16.
    • (1967) Arch. Biochem. Biophys. , vol.122 , pp. 8-16
    • Robyt, J.S.1    French, D.2
  • 2
    • 0014939925 scopus 로고
    • The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme
    • Robyt J.S., French D. The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme. J. Biol. Chem. 245:1970;3917-3927.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3917-3927
    • Robyt, J.S.1    French, D.2
  • 3
    • 0030271795 scopus 로고    scopus 로고
    • Electron microscopic investigation of the diffusion of Bacillus licheniformis α-amylase into corn starch granules
    • Helbert W., Schülein M., Henrissat B. Electron microscopic investigation of the diffusion of Bacillus licheniformis α-amylase into corn starch granules. Int. J. Biol. Macromol. 19:1996;165-169.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 165-169
    • Helbert, W.1    Schülein, M.2    Henrissat, B.3
  • 4
    • 0001879663 scopus 로고
    • Electron microscopy study of the enzymic hydrolysis of Valonia cellulose
    • Chanzy H., Henrissat B. Electron microscopy study of the enzymic hydrolysis of Valonia cellulose. Carbohydr. Polym. 3:1983;161-173.
    • (1983) Carbohydr. Polym. , vol.3 , pp. 161-173
    • Chanzy, H.1    Henrissat, B.2
  • 5
    • 0000028633 scopus 로고
    • Unidirectional degradation of Valonia cellulose microcrystals subjected to cellulase action
    • Chanzy H., Henrissat B. Unidirectional degradation of Valonia cellulose microcrystals subjected to cellulase action. FEBS Letters. 184:1985;285-288.
    • (1985) FEBS Letters , vol.184 , pp. 285-288
    • Chanzy, H.1    Henrissat, B.2
  • 6
    • 0030750573 scopus 로고    scopus 로고
    • Parallel-up structure evidences the molecular directionality during biosynthesis of bacterial cellulose
    • Koyama M., Helbert W., Imai T., Sugiyama J., Henrissat B. Parallel-up structure evidences the molecular directionality during biosynthesis of bacterial cellulose. Proc. Natl Acad. Sci. USA. 94:1997;9091-9095.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9091-9095
    • Koyama, M.1    Helbert, W.2    Imai, T.3    Sugiyama, J.4    Henrissat, B.5
  • 7
    • 0031666637 scopus 로고    scopus 로고
    • Unidirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose mycrocrystals
    • Imai T., Boisset C., Samejima M., Igarashi K., Sugiyama J. Unidirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose mycrocrystals. FEBS Letters. 432:1998;113-116.
    • (1998) FEBS Letters , vol.432 , pp. 113-116
    • Imai, T.1    Boisset, C.2    Samejima, M.3    Igarashi, K.4    Sugiyama, J.5
  • 8
    • 0034029116 scopus 로고    scopus 로고
    • Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A
    • Boisset C., Fraschini C., Schiülein M., Henrissat B., Chanzy H. Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A. Appl. Environ. Microbiol. 66:2000;1444-1451.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1444-1451
    • Boisset, C.1    Fraschini, C.2    Schiülein, M.3    Henrissat, B.4    Chanzy, H.5
  • 9
    • 0037116594 scopus 로고    scopus 로고
    • Directional degradation of beta-chitin by chitinase A1 revealed by a novel reducing end labelling technique
    • Imai T., Watanabe T., Yui T., Sugiyama J. Directional degradation of beta-chitin by chitinase A1 revealed by a novel reducing end labelling technique. FEBS Letters. 510:2002;201-205.
    • (2002) FEBS Letters , vol.510 , pp. 201-205
    • Imai, T.1    Watanabe, T.2    Yui, T.3    Sugiyama, J.4
  • 10
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei
    • Rouvinen J., Bergfors T., Teeri T., Knowles J.K., Jones T.A. Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science. 249:1990;380-386.
    • (1990) Science , vol.249 , pp. 380-386
    • Rouvinen, J.1    Bergfors, T.2    Teeri, T.3    Knowles, J.K.4    Jones, T.A.5
  • 11
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei
    • Divne C., Stahlberg J., Teeri T.T., Jones T.A. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei. J. Mol. Biol. 275:1998;309-325.
    • (1998) J. Mol. Biol. , vol.275 , pp. 309-325
    • Divne, C.1    Stahlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 12
    • 0034687091 scopus 로고    scopus 로고
    • Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action
    • Parsiegla G., Reverbel-Leroy C., Tardif C., Belaich J.P., Driguez H., Haser R. Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action. Biochemistry. 39:2000;11238-11246.
    • (2000) Biochemistry , vol.39 , pp. 11238-11246
    • Parsiegla, G.1    Reverbel-Leroy, C.2    Tardif, C.3    Belaich, J.P.4    Driguez, H.5    Haser, R.6
  • 13
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure. 3:1995;853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 14
    • 0031024813 scopus 로고    scopus 로고
    • A bifunctionalized fluorogenic tetrasaccharide as a substrate to study cellulases
    • Armand S., Drouillard S., Schulein M., Henrissat B., Driguez H. A bifunctionalized fluorogenic tetrasaccharide as a substrate to study cellulases. J. Biol. Chem. 272:1997;2709-2713.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2709-2713
    • Armand, S.1    Drouillard, S.2    Schulein, M.3    Henrissat, B.4    Driguez, H.5
  • 15
    • 0040964309 scopus 로고    scopus 로고
    • Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding
    • Varrot A., Schülein M., Davies G.J. Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding. Biochemistry. 38:1999;8884-8891.
    • (1999) Biochemistry , vol.38 , pp. 8884-8891
    • Varrot, A.1    Schülein, M.2    Davies, G.J.3
  • 16
    • 0033199581 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei
    • Zou J.Y., Kleywegt G.J., Stahlberg J., Driguez H., Nerinckx W., Claeyssens M., et al. Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei. Structure. 7:1999;1035-1045.
    • (1999) Structure , vol.7 , pp. 1035-1045
    • Zou, J.Y.1    Kleywegt, G.J.2    Stahlberg, J.3    Driguez, H.4    Nerinckx, W.5    Claeyssens, M.6
  • 19
    • 0034850147 scopus 로고    scopus 로고
    • A structural basis for processivity
    • Breyer W.A., Matthews B.W. A structural basis for processivity. Protein Sci. 10:2001;1699-1711.
    • (2001) Protein Sci. , vol.10 , pp. 1699-1711
    • Breyer, W.A.1    Matthews, B.W.2
  • 20
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
    • Sakon J., Irwin D., Wilson D.R., Karplus P.A. Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca. Nature Struct. Biol. 4:1997;810-817.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 810-817
    • Sakon, J.1    Irwin, D.2    Wilson, D.R.3    Karplus, P.A.4
  • 21
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • MacGregor E.A., Janeček Š., Svensson B. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta. 1546:2001;1-20.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • Macgregor, E.A.1    Janeček, Š.2    Svensson, B.3
  • 22
    • 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
    • Quian M., Haser R., Buisson G., Duée 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
    • Quian, M.1    Haser, R.2    Buisson, G.3    Duée, E.4    Payan, F.5
  • 23
    • 0030593488 scopus 로고    scopus 로고
    • Carbohydrate and protein-based inhibitors of porcine pancreatic α-amylase: Structure analysis and comparison of their binding characteristics
    • Machius M., Vétersy L., Huber R., Wiegand G. Carbohydrate and protein-based inhibitors of porcine pancreatic α-amylase: structure analysis and comparison of their binding characteristics. J. Mol. Biol. 260:1998;409-421.
    • (1998) J. Mol. Biol. , vol.260 , pp. 409-421
    • Machius, M.1    Vétersy, L.2    Huber, R.3    Wiegand, G.4
  • 25
    • 0035823490 scopus 로고    scopus 로고
    • Changing a single amino acid residue switches processive and non-processive behavior of Aspergillus niger endopolygalacturonase I and II
    • Pagès S., Kester H.C., Visser J., Benen J.A. Changing a single amino acid residue switches processive and non-processive behavior of Aspergillus niger endopolygalacturonase I and II. J. Biol. Chem. 276:2002;33652-33656.
    • (2002) J. Biol. Chem. , vol.276 , pp. 33652-33656
    • Pagès, S.1    Kester, H.C.2    Visser, J.3    Benen, J.A.4
  • 26
    • 0242453826 scopus 로고
    • Carrageenans in the cell walls of Chondrus crispus Stack. (Rhodophyceae, Gigartinales). I Birefringence
    • Gordon-Mills E.M., McCandless E.L. Carrageenans in the cell walls of Chondrus crispus Stack. (Rhodophyceae, Gigartinales). I Birefringence. Phycologia. 16:1977;169-176.
    • (1977) Phycologia , vol.16 , pp. 169-176
    • Gordon-Mills, E.M.1    Mccandless, E.L.2
  • 27
    • 0242622262 scopus 로고
    • Carrageenans in the cell walls of Chondrus crispus Stack. (Rhodophyceae, Gigartinales). II Metachromasy and the optical rotation
    • Gordon-Mills E.M., McCandless E.L. Carrageenans in the cell walls of Chondrus crispus Stack. (Rhodophyceae, Gigartinales). II Metachromasy and the optical rotation. Phycologia. 17:1978;95-104.
    • (1978) Phycologia , vol.17 , pp. 95-104
    • Gordon-Mills, E.M.1    Mccandless, E.L.2
  • 28
    • 0000417027 scopus 로고
    • Structure of the cell walls of marine algae and ecophysiological functions of the matrix polysaccharides
    • Kloareg B., Quatrano R.S. Structure of the cell walls of marine algae and ecophysiological functions of the matrix polysaccharides. Oceanogr. Mar. Biol. Annu. Rev. 26:1988;259-315.
    • (1988) Oceanogr. Mar. Biol. Annu. Rev. , vol.26 , pp. 259-315
    • Kloareg, B.1    Quatrano, R.S.2
  • 29
    • 0014659739 scopus 로고
    • Structure, conformation, and mechanism in the formation of polysaccharide gels and networks
    • Rees D.A. Structure, conformation, and mechanism in the formation of polysaccharide gels and networks. Advan. Carbohydr. Chem. Biochem. 24:1969;267-332.
    • (1969) Advan. Carbohydr. Chem. Biochem. , vol.24 , pp. 267-332
    • Rees, D.A.1
  • 30
    • 0019003158 scopus 로고
    • Cation-specific aggregation of carrageenan helices: Domain model of polymer gel structure
    • Morris E.R., Rees D.A., Robinson G. Cation-specific aggregation of carrageenan helices: domain model of polymer gel structure. J. Mol. Biol. 138:1980;349-362.
    • (1980) J. Mol. Biol. , vol.138 , pp. 349-362
    • Morris, E.R.1    Rees, D.A.2    Robinson, G.3
  • 31
    • 0028462521 scopus 로고
    • On the mechanism of gelation of helix-forming biopolymers
    • Viebke C., Piculell L., Nilsson S. On the mechanism of gelation of helix-forming biopolymers. Macromolecules. 27:1994;4160-4166.
    • (1994) Macromolecules , vol.27 , pp. 4160-4166
    • Viebke, C.1    Piculell, L.2    Nilsson, S.3
  • 32
    • 0001473904 scopus 로고
    • An electron-microscopic study of carrageenan and its interaction with κ-casein
    • Snoeren T.H.M., Both P., Schmidt D.G. An electron-microscopic study of carrageenan and its interaction with κ-casein. Neth. Milk Dairy J. 30:1976;132-141.
    • (1976) Neth. Milk Dairy J. , vol.30 , pp. 132-141
    • Snoeren, T.H.M.1    Both, P.2    Schmidt, D.G.3
  • 34
    • 0016334305 scopus 로고
    • Iota-carrageenan: Molecular structure and packing of polysaccharide double helices in oriented fibers of divalent cation salts
    • Arnott S., Scott W.E., Rees D.A., McNab C.G. Iota-carrageenan: molecular structure and packing of polysaccharide double helices in oriented fibers of divalent cation salts. J. Mol. Biol. 90:1974;253-267.
    • (1974) J. Mol. Biol. , vol.90 , pp. 253-267
    • Arnott, S.1    Scott, W.E.2    Rees, D.A.3    Mcnab, C.G.4
  • 35
    • 0037086321 scopus 로고    scopus 로고
    • Effect of calcium ions on the organization of iota-carrageenan helices: An X-ray investigation
    • Janaswamy S., Chandrasekaran R. Effect of calcium ions on the organization of iota-carrageenan helices: an X-ray investigation. Carbohydr. Res. 337:2002;523-535.
    • (2002) Carbohydr. Res. , vol.337 , pp. 523-535
    • Janaswamy, S.1    Chandrasekaran, R.2
  • 36
    • 0035829075 scopus 로고    scopus 로고
    • Three-dimensional structure of the sodium salt of iota-carrageenan
    • Janaswamy S., Chandrasekaran R. Three-dimensional structure of the sodium salt of iota-carrageenan. Carbohydr. Res. 335:2001;181-194.
    • (2001) Carbohydr. Res. , vol.335 , pp. 181-194
    • Janaswamy, S.1    Chandrasekaran, R.2
  • 37
    • 0015800674 scopus 로고
    • Enzymic hydrolysis of the potassium chloride soluble fraction of carrageenan: Properties of λ-carrageenases from Pseudomonas carrageenovora
    • Johnston K.H., Mc Candless E.L. Enzymic hydrolysis of the potassium chloride soluble fraction of carrageenan: properties of λ-carrageenases from Pseudomonas carrageenovora. Can. J. Microbiol. 19:1973;779-788.
    • (1973) Can. J. Microbiol. , vol.19 , pp. 779-788
    • Johnston, K.H.1    Mc Candless, E.L.2
  • 38
    • 0028230120 scopus 로고
    • The gene encoding the kappa-carrageenase of Alteromonas carrageenovora is related to beta-1,3-1,4-glucanases
    • Barbeyron T., Henrissat B., Kloareg B. The gene encoding the kappa-carrageenase of Alteromonas carrageenovora is related to beta-1,3-1,4-glucanases. Gene. 139:1994;105-109.
    • (1994) Gene , vol.139 , pp. 105-109
    • Barbeyron, T.1    Henrissat, B.2    Kloareg, B.3
  • 39
    • 0031901635 scopus 로고    scopus 로고
    • The kappa-carrageenase of the marine bacterium Cytophaga drobachiensis. Structural and phylogenetic relationships within family-16 glycoside hydrolases
    • Barbeyron T., Gerard A., Potin P., Henrissat B., Kloareg B. The kappa-carrageenase of the marine bacterium Cytophaga drobachiensis. Structural and phylogenetic relationships within family-16 glycoside hydrolases. Mol. Biol. Evol. 15:1998;528-537.
    • (1998) Mol. Biol. Evol. , vol.15 , pp. 528-537
    • Barbeyron, T.1    Gerard, A.2    Potin, P.3    Henrissat, B.4    Kloareg, B.5
  • 40
    • 0034634654 scopus 로고    scopus 로고
    • Iota-carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases
    • Barbeyron T., Michel G., Potin P., Henrissat B., Kloareg B. Iota-carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases. J. Biol. Chem. 275:2000;35499-35505.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35499-35505
    • Barbeyron, T.1    Michel, G.2    Potin, P.3    Henrissat, B.4    Kloareg, B.5
  • 41
    • 0034988224 scopus 로고    scopus 로고
    • The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: A novel insight in the evolution of Clan-B glycoside hydrolases
    • Michel G., Chantalat L., Duee E., Barbeyron T., Henrissat B., Kloareg B., Dideberg O. The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases. Structure. 9:2001;513-525.
    • (2001) Structure , vol.9 , pp. 513-525
    • Michel, G.1    Chantalat, L.2    Duee, E.3    Barbeyron, T.4    Henrissat, B.5    Kloareg, B.6    Dideberg, O.7
  • 42
    • 0027161796 scopus 로고
    • Molecular and active-site structure of a Bacillus 1,3-1,4-β- glucanase
    • Keitel T., Simon O., Borriss R., Heinemann U. Molecular and active-site structure of a Bacillus 1,3-1,4-β-glucanase. Proc. Natl Acad. Sci. USA. 90:1993;5287-5291.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5287-5291
    • Keitel, T.1    Simon, O.2    Borriss, R.3    Heinemann, U.4
  • 43
    • 0035955653 scopus 로고    scopus 로고
    • The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide
    • Michel G., Chantalat L., Fanchon E., Henrissat B., Kloareg B., Dideberg O. The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide. J. Biol. Chem. 276:2001;40202-40209.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40202-40209
    • Michel, G.1    Chantalat, L.2    Fanchon, E.3    Henrissat, B.4    Kloareg, B.5    Dideberg, O.6
  • 44
    • 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
  • 45
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas N.K. Atomic features of protein-carbohydrate interactions. Curr. Opin. Struct. Biol. 1:1991;732-740.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 46
    • 0035957079 scopus 로고    scopus 로고
    • Active-site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis
    • Huang W., Boju L., Tkalec L., Su H., Yang H.-O., Gunay N.R., et al. Active-site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis. Biochemistry. 40:2001;2359-2372.
    • (2001) Biochemistry , vol.40 , pp. 2359-2372
    • Huang, W.1    Boju, L.2    Tkalec, L.3    Su, H.4    Yang, H.-O.5    Gunay, N.R.6
  • 47
    • 0034614498 scopus 로고    scopus 로고
    • The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis
    • Armand S., Wagemaker M.J., Sanchez-Tones P., Kester H.C., van Santen Y., Dijkstra B.W., et al. The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis. J. Biol. Chem. 275:2000;691-696.
    • (2000) J. Biol. Chem. , vol.275 , pp. 691-696
    • Armand, S.1    Wagemaker, M.J.2    Sanchez-Tones, P.3    Kester, H.C.4    Van Santen, Y.5    Dijkstra, B.W.6
  • 48
    • 0042334876 scopus 로고    scopus 로고
    • Dextranase from Penicillium minioluteum: Reaction course. Crystal structure, and product complex
    • Larsson A.M., Andersson R., Ståhlberg J., Kenne L., Jones T.A. Dextranase from Penicillium minioluteum: reaction course. Crystal structure, and product complex. Structure. 11:2003;1111-1121.
    • (2003) Structure , vol.11 , pp. 1111-1121
    • Larsson, A.M.1    Andersson, R.2    Ståhlberg, J.3    Kenne, L.4    Jones, T.A.5
  • 49
    • 0031564610 scopus 로고    scopus 로고
    • Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage
    • Steinbacher S., Miller S., Baxa U., Budisa N., Weintraub A., Seckler R., Huber R. Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage. J. Mol. Biol. 267:1997;865-880.
    • (1997) J. Mol. Biol. , vol.267 , pp. 865-880
    • Steinbacher, S.1    Miller, S.2    Baxa, U.3    Budisa, N.4    Weintraub, A.5    Seckler, R.6    Huber, R.7
  • 50
    • 11944256494 scopus 로고
    • Catalytic mechanisms of glycosyl transfer
    • Sinnott M.L. Catalytic mechanisms of glycosyl transfer. Chem. Rev. 90:1990;1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 51
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 52
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 53
    • 0033525669 scopus 로고    scopus 로고
    • Crystal structure of the thermostable archaeal intron-encoded endonuclease I-DmoI
    • Silva G.H., Dalgaard J.Z., Belfort M., Van Roey P. Crystal structure of the thermostable archaeal intron-encoded endonuclease I-DmoI. J. Mol. Biol. 286:1999;1123-1136.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1123-1136
    • Silva, G.H.1    Dalgaard, J.Z.2    Belfort, M.3    Van Roey, P.4
  • 55
    • 0035443118 scopus 로고    scopus 로고
    • Glycoside hydrolases and glycosyltransferases: Families and functional modules
    • Bourne Y., Henrissat B. Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr. Opin. Struct. Biol. 11:2001;593-600.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 593-600
    • Bourne, Y.1    Henrissat, B.2
  • 56
    • 0002936639 scopus 로고
    • Limiting laws for equilibrium and transport properties of polyelectrolyte solutions
    • E. Selegny, M. Mandel, & U.P. Strauss. Dordrecht, Holland/Boston, USA: D. Riedel Publishing Company
    • Manning G.S. Limiting laws for equilibrium and transport properties of polyelectrolyte solutions. Selegny E., Mandel M., Strauss U.P. Polyelectrolytes. 1974;9-37 D. Riedel Publishing Company, Dordrecht, Holland/Boston, USA.
    • (1974) Polyelectrolytes , pp. 9-37
    • Manning, G.S.1
  • 57
    • 0037478704 scopus 로고    scopus 로고
    • Structural studies for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens
    • Varrot A., Frandsen T.B., von Ossowski I., Boyer V., Cottaz S., Driguez H., et al. Structural studies for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens. Structure. 11:2003;855-864.
    • (2003) Structure , vol.11 , pp. 855-864
    • Varrot, A.1    Frandsen, T.B.2    Von Ossowski, I.3    Boyer, V.4    Cottaz, S.5    Driguez, H.6
  • 58
    • 0034045250 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortis
    • Michel G., Flament D., Barbeyron T., Vernet T., Kloareg B., Dideberg O. Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortis. Acta Crystallog. sect. D. 56:2000;766-768.
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 766-768
    • Michel, G.1    Flament, D.2    Barbeyron, T.3    Vernet, T.4    Kloareg, B.5    Dideberg, O.6
  • 59
    • 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
  • 60
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • Navaza J. Implementation of molecular replacement in AMoRe. Acta Crystallog. sect. D. 57:2001;1367-1372.
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 62
    • 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 Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 63
  • 64
    • 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
  • 66
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallog. sect. D. 55:1999;938-940.
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1


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