메뉴 건너뛰기




Volumn 42, Issue 13, 2003, Pages 3674-3687

Interdependence of backbone flexibility, residue conservation, and enzyme function: A case study on β1,4-Galactosyltransferase-I

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CONFORMATIONS; SOLVENTS; SUBSTRATES;

EID: 0037426326     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034046r     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 0021314461 scopus 로고
    • Structural and functional aspects of domain motions in proteins
    • Bennett, W. S., and Huber, R. (1984) Structural and functional aspects of domain motions in proteins, CRC Crit. Rev. Biochem. 15, 291-384.
    • (1984) CRC Crit. Rev. Biochem. , vol.15 , pp. 291-384
    • Bennett, W.S.1    Huber, R.2
  • 2
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop
    • Joseph, D., Petsko, G. A., and Karplus, M. (1990) Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop, Science 249, 1425-1428.
    • (1990) Science , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 3
    • 0031922657 scopus 로고    scopus 로고
    • Conformational dynamics and enzyme activity
    • Yon, J. M., Perahia, D., and Ghelis, C. (1998) Conformational dynamics and enzyme activity, Biochimie 80, 33-42.
    • (1998) Biochimie , vol.80 , pp. 33-42
    • Yon, J.M.1    Perahia, D.2    Ghelis, C.3
  • 4
    • 0032859140 scopus 로고    scopus 로고
    • Evolution of protein function, from a structural perspective
    • Todd, A. E., Orengo, C. A., and Thornton, J. M. (1999) Evolution of protein function, from a structural perspective, Curr. Opin. Chem. Biol. 3, 548-556.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 548-556
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 5
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar, S., Ma, B., Tsai, C. J., Sinha, N., and Nussinov, R. (2000) Folding and binding cascades: dynamic landscapes and population shifts, Protein Sci. 9, 10-19.
    • (2000) Protein Sci. , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Sinha, N.4    Nussinov, R.5
  • 8
    • 0035903214 scopus 로고    scopus 로고
    • The disordered mobile loop of GroES folds into a defined β-hairpin upon binding GroEL
    • Shewmaker, F., Maskos, K., Simmerling, C., and Landry, S. J. (2001) The disordered mobile loop of GroES folds into a defined β-hairpin upon binding GroEL, J. Biol. Chem. 276, 31257-31264.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31257-31264
    • Shewmaker, F.1    Maskos, K.2    Simmerling, C.3    Landry, S.J.4
  • 9
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young, M. A., Gonfloni, S., Superti-Furga, G., Roux, B., and Kuriyan, J. (2001) Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation, Cell 105, 115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 11
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand, A. J. (2001) Dynamic activation of protein function: A view emerging from NMR spectroscopy, Nat. Struct. Biol. 8, 926-931.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 12
    • 0033117830 scopus 로고    scopus 로고
    • Protein dynamics simulations from nanoseconds to microseconds
    • Doniach, S., and Eastman, P. (1999) Protein dynamics simulations from nanoseconds to microseconds, Curr. Opin. Struct. Biol. 9, 157-163.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 157-163
    • Doniach, S.1    Eastman, P.2
  • 13
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht, A. R., and Daggett, V. (2002) Protein folding and unfolding at atomic resolution, Cell 108, 573-582.
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 14
    • 0012828016 scopus 로고
    • Glycosylation pathway in the biosynthesis of nonreducing terminal sequences in oligosaccharides of glycoproteins
    • Horowitz, M., Ed., Academic Press, New York
    • Beyer, T. A., and Hill, R. L. (1968) Glycosylation pathway in the biosynthesis of nonreducing terminal sequences in oligosaccharides of glycoproteins, in The Glycoconjugates (Horowitz, M., Ed.) Vol. III, pp 25-45, Academic Press, New York.
    • (1968) The Glycoconjugates , vol.3 , pp. 25-45
    • Beyer, T.A.1    Hill, R.L.2
  • 15
    • 0014251737 scopus 로고
    • The role of α-lactalbumin and the A protein in lactose synthetase: A unique mechanism for the control of a biological reaction
    • Brew, K., Vanaman, T. C., and Hill, R. L. (1968) The role of α-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction, Proc. Natl. Acad. Sci. U.S.A. 59, 491-497.
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.59 , pp. 491-497
    • Brew, K.1    Vanaman, T.C.2    Hill, R.L.3
  • 16
    • 0031777054 scopus 로고    scopus 로고
    • The expanding β4-galactosyltransferase gene family: Messages from the databanks
    • Lo, N. W., Shaper, J. H., Pevsner, J., and Shaper, N. L. (1998) The expanding β4-galactosyltransferase gene family: messages from the databanks, Glycobiology 8, 517-526.
    • (1998) Glycobiology , vol.8 , pp. 517-526
    • Lo, N.W.1    Shaper, J.H.2    Pevsner, J.3    Shaper, N.L.4
  • 17
    • 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
  • 18
    • 0032007891 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. (1998) A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities, Biochem. J. 329, 719.
    • (1998) Biochem. J. , vol.329 , pp. 719
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 19
    • 0034675845 scopus 로고    scopus 로고
    • X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: Catalytic mechanism and a new protein superfamily
    • Unligil, U. M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H., and Rini, J. M. (2000) X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily, EMBO J. 19, 5269-5280.
    • (2000) EMBO J. , vol.19 , pp. 5269-5280
    • Unligil, U.M.1    Zhou, S.2    Yuwaraj, S.3    Sarkar, M.4    Schachter, H.5    Rini, J.M.6
  • 20
    • 0033168184 scopus 로고    scopus 로고
    • Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
    • Gastinel, L. N., Cambillau, C., and Bourne, Y. (1999) Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose, EMBO J. 18, 3546-3557.
    • (1999) EMBO J. , vol.18 , pp. 3546-3557
    • Gastinel, L.N.1    Cambillau, C.2    Bourne, Y.3
  • 21
    • 0035967864 scopus 로고    scopus 로고
    • Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the β1,4-galactosyltransferase-I
    • Ramakrishnan, B., and Qasba, P. K. (2001) Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the β1,4-galactosyltransferase-I, J. Mol. Biol. 310, 205-218.
    • (2001) J. Mol. Biol. , vol.310 , pp. 205-218
    • Ramakrishnan, B.1    Qasba, P.K.2
  • 23
    • 0036019552 scopus 로고    scopus 로고
    • Crystal structure of β1,4-galactosyltransferase complex with UDP-gal reveals an oligosaccharide acceptor binding site
    • Ramakrishnan, B., Balaji, P. V., and Qasba, P. K. (2002) Crystal structure of β1,4-galactosyltransferase complex with UDP-gal reveals an oligosaccharide acceptor binding site, J. Mol. Biol. 318, 491-502.
    • (2002) J. Mol. Biol. , vol.318 , pp. 491-502
    • Ramakrishnan, B.1    Balaji, P.V.2    Qasba, P.K.3
  • 24
    • 0019888238 scopus 로고
    • Interactions of substrates and α-lactalbumin with galactosyltransferase as measured by difference spectroscopy
    • Takase, K., and Ebner, K. E. (1981) Interactions of substrates and α-lactalbumin with galactosyltransferase as measured by difference spectroscopy, J. Biol. Chem. 256, 7269-7276.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7269-7276
    • Takase, K.1    Ebner, K.E.2
  • 25
    • 0016631494 scopus 로고
    • Cross-linking of the components of lactose synthetase with dimethylpimelimidate
    • Brew, K., Shaper, J. H., Olsen, K. W., Trayer, I. P., and Hill, R. L. (1975) Cross-linking of the components of lactose synthetase with dimethylpimelimidate, J. Biol. Chem. 250, 1434-1444.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1434-1444
    • Brew, K.1    Shaper, J.H.2    Olsen, K.W.3    Trayer, I.P.4    Hill, R.L.5
  • 27
  • 28
    • 0034308169 scopus 로고    scopus 로고
    • On the unfolding of α-lytic protease and the role of the pro region
    • Inuzuka, Y., and Lazaridis, T. (2000) On the unfolding of α-lytic protease and the role of the pro region, Proteins: Struct., Funct., Genet. 41, 21-32.
    • (2000) Proteins: Struct., Funct., Genet. , vol.41 , pp. 21-32
    • Inuzuka, Y.1    Lazaridis, T.2
  • 29
    • 0037083390 scopus 로고    scopus 로고
    • Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway
    • Sham, Y. Y., Ma, B., Tsai, C. J., and Nussinov, R. (2002) Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway, Proteins: Struct., Funct., Genet., 46, 308-320.
    • (2002) Proteins: Struct., Funct., Genet. , vol.46 , pp. 308-320
    • Sham, Y.Y.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 30
    • 0036533445 scopus 로고    scopus 로고
    • A critical analysis of continuum electrostatics: The screened Coulomb potential-implicit solvent model and the study of the alanine dipeptide and discrimination of misfolded structures of proteins
    • Hassan, S. A., and Mehler, E. L. (2002) A critical analysis of continuum electrostatics: the screened Coulomb potential-implicit solvent model and the study of the alanine dipeptide and discrimination of misfolded structures of proteins, Proteins: Struct., Funct., Genet. 47, 45-61.
    • (2002) Proteins: Struct., Funct., Genet. , vol.47 , pp. 45-61
    • Hassan, S.A.1    Mehler, E.L.2
  • 31
    • 0033531959 scopus 로고    scopus 로고
    • Discrimination of the native from misfolded protein models with an energy function including implicit solvation
    • Lazaridis, T., and Karplus, M. (1999) Discrimination of the native from misfolded protein models with an energy function including implicit solvation, J. Mol. Biol. 288, 477-487.
    • (1999) J. Mol. Biol. , vol.288 , pp. 477-487
    • Lazaridis, T.1    Karplus, M.2
  • 32
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., Ciccotti, G., and Berendsen, H. J. C. (1977) Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes, J. Comput. Phys. 23, 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 33
    • 0042357447 scopus 로고    scopus 로고
    • Potential energy hypersurfaces of nucleotide sugars: Ab initio calculations, force-field parameterization, and exploration of the flexibility
    • Petrova, P., Koca, J., and Imberty, A. (1999) Potential energy hypersurfaces of nucleotide sugars: Ab initio calculations, force-field parameterization, and exploration of the flexibility, J. Am. Chem. Soc. 121, 5535-5547.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5535-5547
    • Petrova, P.1    Koca, J.2    Imberty, A.3
  • 34
    • 0345411345 scopus 로고    scopus 로고
    • Hierarchy of structure loss in MD simulations of src SH3 domain unfolding
    • Tsai, J., Levitt, M., and Baker, D. (1999) Hierarchy of structure loss in MD simulations of src SH3 domain unfolding, J. Mol. Biol. 291, 215-225.
    • (1999) J. Mol. Biol. , vol.291 , pp. 215-225
    • Tsai, J.1    Levitt, M.2    Baker, D.3
  • 36
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and Richards, F. M. (1971) The interpretation of protein structures: estimation of static accessibility, J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 37
    • 0036290392 scopus 로고    scopus 로고
    • A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli
    • Zgiby, S., Plater, A. R., Bates, M. A., Thomson, G. J., and Berry, A. (2002) A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli, J. Mol. Biol. 315, 131-140.
    • (2002) J. Mol. Biol. , vol.315 , pp. 131-140
    • Zgiby, S.1    Plater, A.R.2    Bates, M.A.3    Thomson, G.J.4    Berry, A.5
  • 38
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana, A., Fassina, G., Vita, C., Dalzoppo, D., Zamai, M., and Zambonin, M. (1986) Correlation between sites of limited proteolysis and segmental mobility in thermolysin, Biochemistry 25, 1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.