메뉴 건너뛰기




Volumn 41, Issue 1, 2008, Pages 48-54

Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar

Author keywords

CMP 3FNeuAc; CMP NeuAc; Lactose; PM0188; Sialyltransferase; X ray crystallography

Indexed keywords

PASTEURELLA MULTOCIDA;

EID: 39049156730     PISSN: 12258687     EISSN: 02191024     Source Type: Journal    
DOI: 10.5483/bmbrep.2008.41.1.048     Document Type: Article
Times cited : (25)

References (20)
  • 1
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • Campbell, J. A., Davies, G. J., Bulone, V. and Henrissat, B. (1997) A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 326, 929-939.
    • (1997) Biochem. J , vol.326 , pp. 929-939
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 2
    • 29344431622 scopus 로고    scopus 로고
    • A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries
    • Yu, H., Chokhawala, H., Karpel, R., Yu, H., Wu, B., Zhang, J., Zhang, Y., Jia, Q. and Chen, X. (2005) A multifunctional Pasteurella multocida sialyltransferase: a powerful tool for the synthesis of sialoside libraries. J. Am. Chem. Soc. 127, 17618-17619.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 17618-17619
    • Yu, H.1    Chokhawala, H.2    Karpel, R.3    Yu, H.4    Wu, B.5    Zhang, J.6    Zhang, Y.7    Jia, Q.8    Chen, X.9
  • 3
    • 2442547532 scopus 로고    scopus 로고
    • A case of Pasteurella multocida peritoneal dialysis-associated peritonitis and review of the literature
    • Cooke, F. J., Kodjo, A., Clutterbuck, E. J. and Bamford, K. B. (2004) A case of Pasteurella multocida peritoneal dialysis-associated peritonitis and review of the literature. Int. J. Infect. Dis. 8, 171-174.
    • (2004) Int. J. Infect. Dis , vol.8 , pp. 171-174
    • Cooke, F.J.1    Kodjo, A.2    Clutterbuck, E.J.3    Bamford, K.B.4
  • 6
    • 34249674955 scopus 로고    scopus 로고
    • Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogues reveal substrate binding sites and catalytic mechanism
    • Ni, L., Chokhawala, H. A., Cao, H., Henning, R., Ng, L., Huang, S., Yu, H., Chen, X. and Fisher, A. J. (2007) Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogues reveal substrate binding sites and catalytic mechanism. Biochemistry 46, 6288-6298.
    • (2007) Biochemistry , vol.46 , pp. 6288-6298
    • Ni, L.1    Chokhawala, H.A.2    Cao, H.3    Henning, R.4    Ng, L.5    Huang, S.6    Yu, H.7    Chen, X.8    Fisher, A.J.9
  • 7
    • 33144463744 scopus 로고    scopus 로고
    • Cytidine 5′-monophosphate (CMP)-induced structural changes in a multifunctional sialyltransferase from Pasteurella multocida
    • Ni, L., Sun, M., Yu, H., Chokhawala, H., Chen, X. and Fisher, A. J. (2006) Cytidine 5′-monophosphate (CMP)-induced structural changes in a multifunctional sialyltransferase from Pasteurella multocida. Biochemistry 45, 2139-2148.
    • (2006) Biochemistry , vol.45 , pp. 2139-2148
    • Ni, L.1    Sun, M.2    Yu, H.3    Chokhawala, H.4    Chen, X.5    Fisher, A.J.6
  • 8
    • 0033787822 scopus 로고    scopus 로고
    • Glycosyltransferase structure and mechanism
    • Unligil, U. M. and Rini, J. M. (2000) Glycosyltransferase structure and mechanism. Curr. Opin. Struct. Biol. 10, 510-517.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 510-517
    • Unligil, U.M.1    Rini, J.M.2
  • 9
    • 0037077202 scopus 로고    scopus 로고
    • Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA
    • Pedersen, L. C., Darden, T. A. and Negishi, M. (2002) Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA. J. Biol. Chem. 277, 21869-21873.
    • (2002) J. Biol. Chem , vol.277 , pp. 21869-21873
    • Pedersen, L.C.1    Darden, T.A.2    Negishi, M.3
  • 10
    • 0012784535 scopus 로고    scopus 로고
    • Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
    • Pedersen, L. C., Dong, J., Taniguchi, F., Kitagawa, H., Krahn, J. M., Pedersen, L. G., Sugahara, K. and Negishi, M. (2003) Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. J. Biol. Chem. 278, 14420-14428.
    • (2003) J. Biol. Chem , vol.278 , pp. 14420-14428
    • Pedersen, L.C.1    Dong, J.2    Taniguchi, F.3    Kitagawa, H.4    Krahn, J.M.5    Pedersen, L.G.6    Sugahara, K.7    Negishi, M.8
  • 11
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell, S., Takimoto, T., Portner, A. and Taylor, G. (2000) Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat. Struct. Biol. 7, 1068-1074.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 13
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding
    • Carugo, O. and Argos, P. (1997) NADP-dependent enzymes. I: conserved stereochemistry of cofactor binding. Proteins 28, 10-28.
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 14
    • 33646476008 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the alpha-2,6-sialyltransferase PM0188 from Pasteurella multosida
    • Kim, D. U., Yoo, J. H., Ryu, K. and Cho, H. S. (2006) Crystallization and preliminary X-ray crystallographic analysis of the alpha-2,6-sialyltransferase PM0188 from Pasteurella multosida. Acta crystallogr. F Struct. Biol. Cryst. Commun. 62, 142-144.
    • (2006) Acta crystallogr. F Struct. Biol. Cryst. Commun , vol.62 , pp. 142-144
    • Kim, D.U.1    Yoo, J.H.2    Ryu, K.3    Cho, H.S.4
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in the model
    • Jones, T. A., Zou, J. Y., Cowan, S. W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in the model. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J. and Wodak, S. J. (1999) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55, 191-205.
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 19
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.