메뉴 건너뛰기




Volumn 25, Issue 4, 2006, Pages 434-441

Homology modeling and molecular dynamics study of chorismate synthase from Shigella flexneri

Author keywords

Chorismate synthase; Homology modeling; Molecular dynamics simulation; Protein ligand interaction; Shigella flexneri

Indexed keywords

ANTIBIOTICS; BINDING ENERGY; COMPUTER SIMULATION; MEDICAL PROBLEMS; MICROORGANISMS; MOLECULAR DYNAMICS;

EID: 33751040575     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2006.02.013     Document Type: Article
Times cited : (8)

References (32)
  • 1
    • 33751070156 scopus 로고    scopus 로고
    • WHO/IVR State of the art of new vaccines, Research & Development, Initiative for Vaccine Research, World Health Organization, Geneva, April 2003, p. 74.
  • 2
    • 0032879806 scopus 로고    scopus 로고
    • Global burden of Shigella infections: implications for vaccine development and implementation of control strategies
    • Kottlof K.L., Winickoff J.P., and Ivanoff B. Global burden of Shigella infections: implications for vaccine development and implementation of control strategies. Bull. World Health Org. 77 (1999) 651-666
    • (1999) Bull. World Health Org. , vol.77 , pp. 651-666
    • Kottlof, K.L.1    Winickoff, J.P.2    Ivanoff, B.3
  • 3
    • 33751065499 scopus 로고    scopus 로고
    • D.A. Sack, C. Lyke, C. McLaughlin, Antimicrobial resistancein shigellosis, cholera and campylobacteriosis. World Health Organization/CDS/DRS/2001.8.
  • 4
    • 0032944057 scopus 로고    scopus 로고
    • A unique reaction in a common pathway: mechanism and function of chorismate synthase in the shikimate pathway
    • Macheroux P., Schmid J., Amrhein N., and Schaller A. A unique reaction in a common pathway: mechanism and function of chorismate synthase in the shikimate pathway. Planta 207 (1999) 325-334
    • (1999) Planta , vol.207 , pp. 325-334
    • Macheroux, P.1    Schmid, J.2    Amrhein, N.3    Schaller, A.4
  • 5
    • 0344868502 scopus 로고    scopus 로고
    • The structure of chorismate synthase reveals a novel flavin binding site fundamental to a unique chemical reaction
    • Maclean J., and Ali S. The structure of chorismate synthase reveals a novel flavin binding site fundamental to a unique chemical reaction. Structure 11 (2003) 1499-1511
    • (2003) Structure , vol.11 , pp. 1499-1511
    • Maclean, J.1    Ali, S.2
  • 7
    • 1042275584 scopus 로고    scopus 로고
    • Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights
    • Ahn H.J., Yoon H.J., Lee II B., and Suh S.W. Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights. J. Mol. Biol. 336 (2004) 903-915
    • (2004) J. Mol. Biol. , vol.336 , pp. 903-915
    • Ahn, H.J.1    Yoon, H.J.2    Lee II, B.3    Suh, S.W.4
  • 8
    • 2942547665 scopus 로고    scopus 로고
    • Simulation and modeling of nucleic acid structure, dynamics and interactions
    • Cheatham III T.E. Simulation and modeling of nucleic acid structure, dynamics and interactions. Curr. Opin. Struct. Biol. 14 (2004) 360-367
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 360-367
    • Cheatham III, T.E.1
  • 9
    • 4344691991 scopus 로고    scopus 로고
    • The three-dimensional structure of Arabidopsis thaliana O-methyltransferase predicted by homology-based modeling
    • Yang H., Ahn J.H., Ibrahim R.K., Lee S., and Lim Y. The three-dimensional structure of Arabidopsis thaliana O-methyltransferase predicted by homology-based modeling. J. Mol. Graph. Model 23 (2004) 77-87
    • (2004) J. Mol. Graph. Model , vol.23 , pp. 77-87
    • Yang, H.1    Ahn, J.H.2    Ibrahim, R.K.3    Lee, S.4    Lim, Y.5
  • 10
    • 3042739157 scopus 로고    scopus 로고
    • Theoretical model of the three-dimensional structure of a sugar binding protein from Pyrococcus horikoshii: structural analysis and sugar binding simulations
    • Marabotti A., D'Auria S., Rossi M., and Facchiano A.M. Theoretical model of the three-dimensional structure of a sugar binding protein from Pyrococcus horikoshii: structural analysis and sugar binding simulations. Biochem. J. 380 (2004) 677-684
    • (2004) Biochem. J. , vol.380 , pp. 677-684
    • Marabotti, A.1    D'Auria, S.2    Rossi, M.3    Facchiano, A.M.4
  • 11
    • 24944573556 scopus 로고    scopus 로고
    • Structural model of the Plasmodium CDK, Pfmrk, a novel target for malaria therapeutics
    • Peng Y., Keenan S.M., and Welsh W.J. Structural model of the Plasmodium CDK, Pfmrk, a novel target for malaria therapeutics. J. Mol. Graph. Model 24 (2005) 72-80
    • (2005) J. Mol. Graph. Model , vol.24 , pp. 72-80
    • Peng, Y.1    Keenan, S.M.2    Welsh, W.J.3
  • 14
    • 0348047617 scopus 로고    scopus 로고
    • Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology
    • Viola C.M., Saridakis V., and Christendat D. Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology. Proteins 54 (2004) 166-169
    • (2004) Proteins , vol.54 , pp. 166-169
    • Viola, C.M.1    Saridakis, V.2    Christendat, D.3
  • 16
    • 0030825816 scopus 로고    scopus 로고
    • Protein residue colour references
    • Online:
    • Taylor W.R. Protein residue colour references. Protein Eng. 10 (1997) 743-746. http://emboss.sourceforge.net/Jemboss/jae.html Online:
    • (1997) Protein Eng. , vol.10 , pp. 743-746
    • Taylor, W.R.1
  • 17
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 18
    • 0035961045 scopus 로고    scopus 로고
    • A theoretical study of the chorismate synthase reaction
    • Dmitrenko O., Wood H.B., Bach R.D., and Ganem B. A theoretical study of the chorismate synthase reaction. Org. Lett. 3 (2001) 4137-4140
    • (2001) Org. Lett. , vol.3 , pp. 4137-4140
    • Dmitrenko, O.1    Wood, H.B.2    Bach, R.D.3    Ganem, B.4
  • 19
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 22
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for determining atom-centered charges: the RESP model
    • Bayly C.I., Cieplak P., Cornell W.D., and Kollman P.A. A well-behaved electrostatic potential based method using charge restraints for determining atom-centered charges: the RESP model. J. Phys. Chem. 97 (1993) 10269
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 23
    • 0033198021 scopus 로고    scopus 로고
    • A molecular dynamics simulation of the flavin mononucleotide-RNA aptamer complex
    • Schneider C., and Suhnel J. A molecular dynamics simulation of the flavin mononucleotide-RNA aptamer complex. Biopolymers 50 (1999) 287-302
    • (1999) Biopolymers , vol.50 , pp. 287-302
    • Schneider, C.1    Suhnel, J.2
  • 24
    • 33751062080 scopus 로고    scopus 로고
    • D.A. Case, T.A. Darden, T.E. Cheatham III, C.L. Simmerling, J. Wang, R.E. Duke, R. Luo, K.M. Merz, B. Wang, D.A. Pearlman, M. Crowley, S. Brozell, V. Tsui, H. Gohlke, J. Mongan, V. Hornak, G. Cui, P. Beroza, C. Schafmeister, J.W. Caldwell, W.S. Ross, P.A. Kollman, AMBER8 University of California, San Francisco, 2004.
  • 26
    • 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. Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes. J. Comput. Phys. 23 (1977) 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 27
    • 0034084991 scopus 로고    scopus 로고
    • Combined molecular mechanical and continuum solvent approach (MM-PBSA/GBSA) to predict ligand binding
    • Massova I., and Kollman P.A. Combined molecular mechanical and continuum solvent approach (MM-PBSA/GBSA) to predict ligand binding. Perspect. Drug Discov. 18 (2000) 113-135
    • (2000) Perspect. Drug Discov. , vol.18 , pp. 113-135
    • Massova, I.1    Kollman, P.A.2
  • 28
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized Born solvation model in macromolecular simulations
    • Tsui V., and Case D.A. Theory and applications of the generalized Born solvation model in macromolecular simulations. Biopolymers 56 (2001) 275-291
    • (2001) Biopolymers , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 29
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser J., Shenkin P.S., and Still W.C. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO). J. Comput. Chem. 20 (1999) 217-230
    • (1999) J. Comput. Chem. , vol.20 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 30
    • 0034682881 scopus 로고    scopus 로고
    • An integrated approach to the analysis and modeling of protein sequences and structures
    • Yang A.S., and Honig B. An integrated approach to the analysis and modeling of protein sequences and structures. J. Mol. Biol. 301 (2000) 665-711
    • (2000) J. Mol. Biol. , vol.301 , pp. 665-711
    • Yang, A.S.1    Honig, B.2
  • 31
    • 21244436719 scopus 로고    scopus 로고
    • Homology modeling and molecular dynamics simulations of transmembrane domain structure of human neuronal nicotinic acetylcholine receptor
    • Alexander C.S., Yan X., and Pei T. Homology modeling and molecular dynamics simulations of transmembrane domain structure of human neuronal nicotinic acetylcholine receptor. Biophys. J. 88 (2005) 1009-1017
    • (2005) Biophys. J. , vol.88 , pp. 1009-1017
    • Alexander, C.S.1    Yan, X.2    Pei, T.3
  • 32
    • 22644447155 scopus 로고    scopus 로고
    • Theoretical investigation of normal to strong hydrogen bonds
    • Pak C., Lee H.M., Kim J.C., Kim D., and Kim K.S. Theoretical investigation of normal to strong hydrogen bonds. Struct. Chem. 16 (2005) 187-202
    • (2005) Struct. Chem. , vol.16 , pp. 187-202
    • Pak, C.1    Lee, H.M.2    Kim, J.C.3    Kim, D.4    Kim, K.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.