메뉴 건너뛰기




Volumn 9, Issue 3, 2000, Pages 544-551

The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis

Author keywords

Beta alpha barrel; Chitinase; Fungal pathogen; Mutagenesis; X ray structure

Indexed keywords

CHITINASE;

EID: 0034064512     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.3.544     Document Type: Article
Times cited : (109)

References (39)
  • 1
    • 0030115305 scopus 로고    scopus 로고
    • Emerging disease issues and fungal pathogens associated with HIV infection
    • Ampel NM. 1996. Emerging disease issues and fungal pathogens associated with HIV infection. Emerg Infect Dis 2:109-116.
    • (1996) Emerg Infect Dis , vol.2 , pp. 109-116
    • Ampel, N.M.1
  • 2
    • 0028316274 scopus 로고
    • Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulons WL-12
    • Armand S, Tomita H, Heyraud A, Gey C, Watanabe T, Henrissat B. 1994. Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulons WL-12. FEBS Lett 343:177-180.
    • (1994) FEBS Lett , vol.343 , pp. 177-180
    • Armand, S.1    Tomita, H.2    Heyraud, A.3    Gey, C.4    Watanabe, T.5    Henrissat, B.6
  • 3
    • 0026761188 scopus 로고
    • Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: Similarity to bacterial chitinases
    • Blaiseau PL, Lafay JF. 1992. Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: Similarity to bacterial chitinases. Gene 120:243-248.
    • (1992) Gene , vol.120 , pp. 243-248
    • Blaiseau, P.L.1    Lafay, J.F.2
  • 5
    • 0032584768 scopus 로고    scopus 로고
    • Substrate assistance in the mechanism of family 18 chitinases: Theoretical studies of potential intermediates and inhibitors
    • Brameld KA, Shrader WD, Imperiali B, Goddard WA III. 1998. Substrate assistance in the mechanism of family 18 chitinases: Theoretical studies of potential intermediates and inhibitors. J Mol Biol 250:913-923.
    • (1998) J Mol Biol , vol.250 , pp. 913-923
    • Brameld, K.A.1    Shrader, W.D.2    Imperiali, B.3    Goddard W.A. III4
  • 6
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brünger AT. 1990. Extension of molecular replacement: A new search strategy based on Patterson correlation refinement. Acta Crystallogr A446:46-57.
    • (1990) Acta Crystallogr , vol.A446 , pp. 46-57
    • Brünger, A.T.1
  • 8
    • 0000127585 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value
    • Brünger AT. 1993. Assessment of phase accuracy by cross validation: The free R value. Acta Crystallogr D49:129-147.
    • (1993) Acta Crystallogr , vol.D49 , pp. 129-147
    • Brünger, A.T.1
  • 9
    • 0025169558 scopus 로고
    • Chitin synthase I and chitin synthase II are not required for chitin synthesis in vivo in Saccharomyces cerevisiae
    • Bulawa CE, Osmond BC. 1990. Chitin synthase I and chitin synthase II are not required for chitin synthesis in vivo in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 87:7424-7428.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7424-7428
    • Bulawa, C.E.1    Osmond, B.C.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (Collaborative Computational Project Number 4). 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 11
    • 0000775077 scopus 로고
    • Conidia of Coccidioides immitis their significance in disease initiation
    • Cole GT, Hoch HC, eds. New York: Plenum Press
    • Cole GT. Kirkland TN. 1991. Conidia of Coccidioides immitis their significance in disease initiation. In: Cole GT, Hoch HC, eds. The fungal spore and disease initiation in plants and animals. New York: Plenum Press. pp 403-443.
    • (1991) The Fungal Spore and Disease Initiation in Plants and Animals , pp. 403-443
    • Cole, G.T.1    Kirkland, T.N.2
  • 12
    • 0025905975 scopus 로고
    • Production and characterization of a monoclonal antibody to the complement fixation antigen of Coccidioides immitis
    • Dolan MJ, Cox RA. 1991. Production and characterization of a monoclonal antibody to the complement fixation antigen of Coccidioides immitis. Infect Immun 59:2175-2180.
    • (1991) Infect Immun , vol.59 , pp. 2175-2180
    • Dolan, M.J.1    Cox, R.A.2
  • 13
    • 0028135314 scopus 로고
    • Cloning and characterization of a chitinase (chit42) cDNA from the mycoparasitic fungus Trichoderma harzianum
    • Garcia I, Lora JM, de la Cruz J, Benitez T, Llobell A, Pintor-Toro JA. 1994. Cloning and characterization of a chitinase (chit42) cDNA from the mycoparasitic fungus Trichoderma harzianum. Curr Genet 27:83-89.
    • (1994) Curr Genet , vol.27 , pp. 83-89
    • Garcia, I.1    Lora, J.M.2    De La Cruz, J.3    Benitez, T.4    Llobell, A.5    Pintor-Toro, J.A.6
  • 14
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. Seeds at 1.8 Å resolution
    • Hart PJ, Pfluger HD, Monzingo AF, Hollis T, Robertus JD. 1995. The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 Å resolution. J Mol Biol 248:402-413.
    • (1995) J Mol Biol , vol.248 , pp. 402-413
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 15
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293:781-788.
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 16
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins DG, Bleasby AJ, Fuchs R. 1992. CLUSTAL V: Improved software for multiple sequence alignment. Comput Appl Biosci 8:189-191.
    • (1992) Comput Appl Biosci , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 18
    • 0032213231 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a chitinase from the fungal pathogen Coccidioides immitis
    • Hollis T, Monzingo AF, Bortone K, Schelp E, Cox R, Robertus JD. 1998. Crystallization and preliminary X-ray analysis of a chitinase from the fungal pathogen Coccidioides immitis. Acta Crystallogr D54:1412-1413.
    • (1998) Acta Crystallogr , vol.D54 , pp. 1412-1413
    • Hollis, T.1    Monzingo, A.F.2    Bortone, K.3    Schelp, E.4    Cox, R.5    Robertus, J.D.6
  • 19
    • 0026724813 scopus 로고
    • The coccidioidal complement fixation and immunodiffusion-complement fixation antigen is a chitinase
    • Johnson SM, Pappagianis D. 1992. The coccidioidal complement fixation and immunodiffusion-complement fixation antigen is a chitinase. Infect Immun 60:2588-2592.
    • (1992) Infect Immun , vol.60 , pp. 2588-2592
    • Johnson, S.M.1    Pappagianis, D.2
  • 20
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
    • Jones JDG, Grady KL, Suslow TV, Bedbrook JR. 1986. Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J 5:467-473.
    • (1986) EMBO J , vol.5 , pp. 467-473
    • Jones, J.D.G.1    Grady, K.L.2    Suslow, T.V.3    Bedbrook, J.R.4
  • 21
    • 0001797984 scopus 로고
    • FRODO: A graphics fitting program for macromolecules
    • Sayer D, ed. Oxford: Clarendon Press
    • Jones TA. 1982. FRODO: A graphics fitting program for macromolecules. In: Sayer D, ed. Computational crystallography. Oxford: Clarendon Press. pp 303-317.
    • (1982) Computational Crystallography , pp. 303-317
    • Jones, T.A.1
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0030498233 scopus 로고    scopus 로고
    • Xd1MAPMAN and xd1DATAMAN - Programs for reformatting analysis and manipulation of biomolecular electron-density maps and reflection data sets
    • Kleywegt GJ, Jones TA. 1996. xd1MAPMAN and xd1DATAMAN - Programs for reformatting analysis and manipulation of biomolecular electron-density maps and reflection data sets. Acta Crystallogr D52:826-828.
    • (1996) Acta Crystallogr , vol.D52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda MJ, Robbins PW. 1991. Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J Biol Chem 266:19758-19767.
    • (1991) J Biol Chem , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 26
  • 27
    • 84977303434 scopus 로고
    • R-free likelihood-based estimates of errors for phases calculated from atomic models
    • Lunin VY, Skovoroda TD. 1995. R-free likelihood-based estimates of errors for phases calculated from atomic models. Acta Crystallogr A51:880-886.
    • (1995) Acta Crystallogr , vol.A51 , pp. 880-886
    • Lunin, V.Y.1    Skovoroda, T.D.2
  • 28
    • 0027077821 scopus 로고
    • Chemical modification studies of the active centre of Candida albicans chitinase and its inhibition by allosamidin
    • Milewski S, O'Donnell RW, Gooday GW. 1992. Chemical modification studies of the active centre of Candida albicans chitinase and its inhibition by allosamidin. J Gen Microbiol 138:2545-2550.
    • (1992) J Gen Microbiol , vol.138 , pp. 2545-2550
    • Milewski, S.1    O'Donnell, R.W.2    Gooday, G.W.3
  • 29
    • 0030978629 scopus 로고    scopus 로고
    • Fungal infections in patients with acquired immunodeficiency syndrom
    • Minamoto GY, Rosenberg AS. 1997. Fungal infections in patients with acquired immunodeficiency syndrom. Med Clin North Am 81:381-409.
    • (1997) Med Clin North Am , vol.81 , pp. 381-409
    • Minamoto, G.Y.1    Rosenberg, A.S.2
  • 30
    • 0030032332 scopus 로고    scopus 로고
    • Chitinases chitosanases and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core
    • Monzingo AF, Marcotte EM, Hart PJ, Robertus JD. 1996. Chitinases chitosanases and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core. Nat Struct Biol 3:133-140.
    • (1996) Nat Struct Biol , vol.3 , pp. 133-140
    • Monzingo, A.F.1    Marcotte, E.M.2    Hart, P.J.3    Robertus, J.D.4
  • 31
  • 34
    • 0029558952 scopus 로고
    • Isolation and characterization of two chitinase-encoding genes (cts1 cts2) from the fungus Coccidioides immitis
    • Pishko EJ, Kirkland TN, Cole GT. 1995. Isolation and characterization of two chitinase-encoding genes (cts1 cts2) from the fungus Coccidioides immitis. Gene 167:173-177.
    • (1995) Gene , vol.167 , pp. 173-177
    • Pishko, E.J.1    Kirkland, T.N.2    Cole, G.T.3
  • 35
    • 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 AC, Armand S, Kalk KH, Isogai A, Henrissat B, Dijkstra BW. 1995. Stereochemistry of chitin hydrolysis by a plant chitinase/ lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis. Biochemistry 34:15619-5623.
    • (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
  • 36
    • 0030595119 scopus 로고    scopus 로고
    • The 1.8 Å resolution structure of hevamine a plant chitinase/lysozyme and analysis of the conserved sequence and: Structure motifs of glycosyl hydrolase family 18
    • Terwisscha van Scheltinga AC, Hennig M, Dijkstra BW. 1996. The 1.8 Å 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
    • Terwisscha Van Scheltinga, A.C.1    Hennig, M.2    Dijkstra, B.W.3
  • 37
    • 2542598433 scopus 로고    scopus 로고
    • A procedure compatible with X-PLOR for the calculation of electron-density maps weighted using an R-free-likelihood approach
    • Urzhumtsev AG, Skovoroda TD, Lunin VY. 1996. A procedure compatible with X-PLOR for the calculation of electron-density maps weighted using an R-free-likelihood approach. J Appl Crystallogr 29:741-744.
    • (1996) J Appl Crystallogr , vol.29 , pp. 741-744
    • Urzhumtsev, A.G.1    Skovoroda, T.D.2    Lunin, V.Y.3
  • 38
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulons WL-12 as essential residues for chitinase activity
    • Watanabe T, Kobori K, Miyashita K, Fujii T, Sakai H, Uchida M, Tanaka H. 1993. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulons WL-12 as essential residues for chitinase activity. J Biol Chem 268:18567-18572.
    • (1993) J Biol Chem , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 39
    • 0029949505 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the Coccidioides immitis complement fixation/chitinase antigen
    • Yang C, Zhu Y, Magee DM, Cox RA. 1996. Molecular cloning and characterization of the Coccidioides immitis complement fixation/chitinase antigen. Infect Immun 64:1992-1997.
    • (1996) Infect Immun , vol.64 , pp. 1992-1997
    • Yang, C.1    Zhu, Y.2    Magee, D.M.3    Cox, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.