메뉴 건너뛰기




Volumn 155, Issue 2, 2014, Pages 115-122

Solution structure of the chitin-binding domain 1 (ChBD1) of a hyperthermophilic chitinase from Pyrococcus furiosus

Author keywords

carbohydrate binding module; CBM family 5; chitin binding domain; Chitinase

Indexed keywords

CARBOHYDRATE BINDING PROTEIN; CHITIN; CHITIN BINDING DOMAIN 1; CHITINASE; UNCLASSIFIED DRUG;

EID: 84893288464     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvt104     Document Type: Article
Times cited : (12)

References (30)
  • 2
    • 33746449573 scopus 로고    scopus 로고
    • Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: Activity toward crystalline chitin
    • Oku, T. and Ishikawa, K. (2006) Analysis of the hyperthermophilic chitinase from Pyrococcus furiosus: activity toward crystalline chitin. Biosci. Biotechnol. Biochem. 70, 1696-1701
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1696-1701
    • Oku, T.1    Ishikawa, K.2
  • 6
    • 0031406028 scopus 로고    scopus 로고
    • Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi
    • Brun, E., Moriaud, F., Gans, P., Blackledge, M.J., Barras, F., and Marion, D. (1997) Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi. Biochemistry 36, 16074-16086
    • (1997) Biochemistry , vol.36 , pp. 16074-16086
    • Brun, E.1    Moriaud, F.2    Gans, P.3    Blackledge, M.J.4    Barras, F.5    Marion, D.6
  • 7
    • 25444447367 scopus 로고    scopus 로고
    • GASH: An improved algorithm for maximizing the number of equivalent residues between two protein structures
    • Standley, D.M., Toh, H., and Nakamura, H. (2005) GASH: An improved algorithm for maximizing the number of equivalent residues between two protein structures. BMC Bioinformatics 6, 221
    • (2005) BMC Bioinformatics , vol.6 , pp. 221
    • Standley, D.M.1    Toh, H.2    Nakamura, H.3
  • 9
    • 47849085074 scopus 로고    scopus 로고
    • Tertiary structure and carbohydrate recognition by the chitin-binding domain of a hyperthermophilic chitinase from Pyrococcus furiosus
    • Nakamura, T., Mine, S., Hagihara, Y., Ishikawa, K., Ikegami, T., and Uegaki, K. (2008) Tertiary structure and carbohydrate recognition by the chitin-binding domain of a hyperthermophilic chitinase from Pyrococcus furiosus. J. Mol. Biol. 381, 670-680
    • (2008) J. Mol. Biol. , vol.381 , pp. 670-680
    • Nakamura, T.1    Mine, S.2    Hagihara, Y.3    Ishikawa, K.4    Ikegami, T.5    Uegaki, K.6
  • 10
    • 84877245601 scopus 로고    scopus 로고
    • Structure of a complete four-domain chitinase from Moritella marina, a marine psychrophilic bacterium
    • Malecki, P.H., Raczynska, J.E., Vorgias, C.E., and Rypniewski, W. (2013) Structure of a complete four-domain chitinase from Moritella marina, a marine psychrophilic bacterium. Acta Crystallogr. D 69, 821-829
    • (2013) Acta Crystallogr. D , vol.69 , pp. 821-829
    • Malecki, P.H.1    Raczynska, J.E.2    Vorgias, C.E.3    Rypniewski, W.4
  • 11
    • 0024435833 scopus 로고
    • Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling
    • Neri, D., Szyperski, T., Otting, G., Senn, H., and Wuthrich, K. (1989) Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. Biochemistry 28, 7510-7516
    • (1989) Biochemistry , vol.28 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wuthrich, K.5
  • 12
    • 12044258763 scopus 로고
    • Two-dimensional NMR experiments for correlating 13Cb and 1H"/d chemical shifts of aromatic residues in 13Clabeled proteins via scalar couplings
    • Yamazaki, T., Formankay, J.D., and Kay, L.E. (1993) Two-dimensional NMR experiments for correlating 13Cb and 1H"/d chemical shifts of aromatic residues in 13Clabeled proteins via scalar couplings. J. Am. Chem. Soc. 115, 11054-11055
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11054-11055
    • Yamazaki, T.1    Formankay, J.D.2    Kay, L.E.3
  • 13
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 14
    • 84871444338 scopus 로고    scopus 로고
    • University of California San Francisco
    • Goddard, T.D. and Kneller, D.G. (2008) SPARKY 3. University of California, San Francisco
    • (2008) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 15
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., Mumenthaler, C., and Wuthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 16
    • 68349093958 scopus 로고    scopus 로고
    • TALOS plus: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) TALOS plus: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 17
    • 0030981418 scopus 로고    scopus 로고
    • Two-dimensional NMR methods for determining-1 angles of aromatic residues in proteins from three-bond JC'Cg and JNCg couplings
    • Hu, J.S., Grzesiek, S., and Bax, A. (1997) Two-dimensional NMR methods for determining-1 angles of aromatic residues in proteins from three-bond JC'Cg and JNCg couplings. J. Am. Chem. Soc. 119, 1803-1804
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1803-1804
    • Hu, J.S.1    Grzesiek, S.2    Bax, A.3
  • 18
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Kaptein, R., and Thornton, J.M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 21
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo, J., Lamed, R., Chirino, A.J., Morag, E., Bayer, E.A., Shoham, Y., and Steitz, T.A. (1996) Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 15, 5739-5751
    • (1996) EMBO J. , vol.15 , pp. 5739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morag, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 22
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston, A.B., Bolam, D.N., Gilbert, H.J., and Davies, G.J. (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382, 769-781
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 23
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase i from Trichoderma reesei A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • Kraulis, J., Clore, G.M., Nilges, M., Jones, T.A., Pettersson, G., Knowles, J., and Gronenborn, A.M. (1989) Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 28, 7241-7257
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 24
  • 26
    • 33749827454 scopus 로고    scopus 로고
    • Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C
    • Itoh, Y., Watanabe, J., Fukada, H., Mizuno, R., Kezuka, Y., Nonaka, T., and Watanabe, T. (2006) Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C. Appl. Microbiol. Biotechnol. 72, 1176-1184
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 1176-1184
    • Itoh, Y.1    Watanabe, J.2    Fukada, H.3    Mizuno, R.4    Kezuka, Y.5    Nonaka, T.6    Watanabe, T.7
  • 27
    • 84859045253 scopus 로고    scopus 로고
    • Mutational analysis of a CBM family 5 chitin-binding domain of an alkaline chitinase from Bacillus sp. J813
    • Uni, F., Lee, S., Yatsunami, R., Fukui, T., and Nakamura, S. (2012) Mutational analysis of a CBM family 5 chitin-binding domain of an alkaline chitinase from Bacillus sp. J813. Biosci. Biotechnol. Biochem. 76, 530-535
    • (2012) Biosci. Biotechnol. Biochem. , vol.76 , pp. 530-535
    • Uni, F.1    Lee, S.2    Yatsunami, R.3    Fukui, T.4    Nakamura, S.5
  • 28
    • 84880968149 scopus 로고    scopus 로고
    • Involvement of Gln679, in addition to Trp687, in chitin-binding activity of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12
    • Hara, M., Sugimoto, H., Uemura, M., Akagi, K., Suzuki, K., Ikegami, T., and Watanabe, T. (2013) Involvement of Gln679, in addition to Trp687, in chitin-binding activity of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12. J. Biochem. 154, 185-193
    • (2013) J. Biochem. , vol.154 , pp. 185-193
    • Hara, M.1    Sugimoto, H.2    Uemura, M.3    Akagi, K.4    Suzuki, K.5    Ikegami, T.6    Watanabe, T.7
  • 29
    • 33846049457 scopus 로고    scopus 로고
    • Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus
    • Nakamura, T., Mine, S., Hagihara, Y., Ishikawa, K., and Uegaki, K. (2007) Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus. Acta Crystallogr. F 63, 7-11
    • (2007) Acta Crystallogr. F , vol.63 , pp. 7-11
    • Nakamura, T.1    Mine, S.2    Hagihara, Y.3    Ishikawa, K.4    Uegaki, K.5
  • 30
    • 77953183572 scopus 로고    scopus 로고
    • Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus-The role of conserved residues in the active site
    • Tsuji, H., Nishimura, S., Inui, T., Kado, Y., Ishikawa, K., Nakamura, T., and Uegaki, K. (2010) Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus-the role of conserved residues in the active site. FEBS J. 277, 2683-2695
    • (2010) FEBS J. , vol.277 , pp. 2683-2695
    • Tsuji, H.1    Nishimura, S.2    Inui, T.3    Kado, Y.4    Ishikawa, K.5    Nakamura, T.6    Uegaki, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.