메뉴 건너뛰기




Volumn 33, Issue 6, 2015, Pages 1198-1210

An in silico structural insights into Plasmodium LytB protein and its inhibition

Author keywords

drug target; IspH; LytB; non mevalonate pathway; virtual screening

Indexed keywords

ANTIMALARIAL AGENT; ENZYME INHIBITOR; LIGAND; PROTOZOAL PROTEIN;

EID: 84939884063     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2014.938248     Document Type: Article
Times cited : (7)

References (71)
  • 2
    • 70350033518 scopus 로고    scopus 로고
    • Structural model of the Plasmodium falciparum Thioredoxin reductase: A novel target for antimalarial drugs
    • Retrieved from
    • Banerjee, A. K., Arora, N., Murty, U. S. N. (2009). Structural model of the Plasmodium falciparum Thioredoxin reductase: A novel target for antimalarial drugs. Journal of Vector Borne Diseases, 46, 171-183. Retrieved from http://www.mrcindia.org/
    • (2009) Journal of Vector Borne Diseases , vol.46 , pp. 171-183
    • Banerjee, A.K.1    Arora, N.2    Murty, U.S.N.3
  • 4
    • 0026639957 scopus 로고
    • Sterol molecule: Structure, biosyn thesis and function
    • Bloch, K. (1992). Sterol molecule: Structure, biosynthesis, and function. Steroids, 57, 378-383.
    • (1992) Steroids , vol.57 , pp. 378-383
    • Bloch, K.1
  • 8
    • 0032132839 scopus 로고    scopus 로고
    • Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits1
    • Bouvier, F., dHarlingue, A., Suire, C., Backhaus, R. A., Camara, B. (1998). Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits1. Plant Physiology, 117, 1423-1431.
    • (1998) Plant Physiology , vol.117 , pp. 1423-1431
    • Bouvier, F.1    Harlingue, A.2    Suire, C.3    Backhaus, R.A.4    Camara, B.5
  • 11
    • 0028837082 scopus 로고
    • Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants
    • Chappell, J. (1995). Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants. Annual Review of Plant Physiology and Plant Molecular Biology, 46, 521-547.
    • (1995) Annual Review of Plant Physiology and Plant Molecular Biology , vol.46 , pp. 521-547
    • Chappell, J.1
  • 13
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • Colovos, C., Yeates, T. O. (1993). Verification of protein structures: Patterns of nonbonded atomic interactions. Protein Science, 2, 1511-1519.
    • (1993) Protein Science , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 14
    • 0003068398 scopus 로고
    • Major animal models in malaria research: Rodent
    • In W. H. Wernsdorfer, & I. McGregor. (Eds) London: Churchill Livingstone
    • Cox, F. E. G. (1988). Major animal models in malaria research: Rodent. In W. H. Wernsdorfer, & I. McGregor. (Eds.), Malaria: Principles and practice of malariology (pp. 1503-1543). London: Churchill Livingstone.
    • (1988) Malaria: Principles and Practice of Malariology , pp. 1503-1543
    • Cox, F.E.G.1
  • 15
    • 0002317514 scopus 로고    scopus 로고
    • Natural products (secondary metabolites
    • In B. Buchanan, W. Gruissem, R. Jones, & M. Dekker. (Eds) New York, NY: American Society of Plant Physiologists
    • Croteau, R., Kutchan, T. M., Lewis, N. G. (2000). Natural products (secondary metabolites). In B. Buchanan, W. Gruissem, R. Jones, & M. Dekker. (Eds.), Biochemistry & molecular biology of plants (pp. 1250-1318). New York, NY: American Society of Plant Physiologists.
    • (2000) Biochemistry & Molecular Biology of Plants , pp. 1250-1318
    • Croteau, R.1    Kutchan, T.M.2    Lewis, N.G.3
  • 16
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An Nslog(N) method for Ewald sums in large systems
    • Darden, T., York, D., Pedersen, L. (1993). Particle mesh Ewald: An Nslog(N) method for Ewald sums in large systems. The Journal of Chemical Physics, 98, 10089-10092.
    • (1993) The Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 19
  • 20
    • 0035947595 scopus 로고    scopus 로고
    • Chemical synthesis and biological activity of bromohydrin pyrophosphate, a potent stimulator of human gamma delta T Cells
    • Espinosa, E., Belmant, C., Pont, F., Luciani, B., Poupot, R., Romagné, F.,., Fournié, J. J. (2001). Chemical synthesis and biological activity of bromohydrin pyrophosphate, a potent stimulator of human gamma delta T Cells. Journal of Biological Chemistry, 276, 18337-18344.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 18337-18344
    • Espinosa, E.1    Belmant, C.2    Pont, F.3    Luciani, B.4    Poupot, R.5    Romagné, F.6    Fournié, J.J.7
  • 22
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L., Brown, M. S. (1990). Regulation of the mevalonate pathway. Nature, 343, 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 26
    • 84859418111 scopus 로고    scopus 로고
    • The MEP pathway and the development of inhibitors as potential anti-infective agents
    • Hale, I., ONeill, P. M., Berry, N. G., Odom, A., Sharma, R. (2012). The MEP pathway and the development of inhibitors as potential anti-infective agents. Med Chem Comm, 3, 418-433.
    • (2012) Med Chem Comm , vol.3 , pp. 418-433
    • Hale, I.1    Oneill, P.M.2    Berry, N.G.3    Odom, A.4    Sharma, R.5
  • 30
    • 34548409606 scopus 로고    scopus 로고
    • Drug-resistant malaria-An insight
    • Hyde, J. E. (2007). Drug-resistant malaria-An insight. FEBS Journal, 274, 4688-4698.
    • (2007) FEBS Journal , vol.274 , pp. 4688-4698
    • Hyde, J.E.1
  • 32
    • 0027497370 scopus 로고
    • Probing the pyrophosphate-binding site in potato tuber UDP-glucose pyrophosphorylase with pyridoxal diphosphate
    • Kazuta, Y., Tagaya, M., Tanizawa, K., Fukui, T. (1993). Probing the pyrophosphate-binding site in potato tuber UDP-glucose pyrophosphorylase with pyridoxal diphosphate. Protein Science, 2, 119-125.
    • (1993) Protein Science , vol.2 , pp. 119-125
    • Kazuta, Y.1    Tagaya, M.2    Tanizawa, K.3    Fukui, T.4
  • 33
    • 0343614184 scopus 로고    scopus 로고
    • A family of transketolases that directs isoprenoid biosynthesis via a mevalonate-independent pathway
    • Retrieved from
    • Lange, B. M., Wildung, M. R., McCaskill, D., Croteau, R. (1998). A family of transketolases that directs isoprenoid biosynthesis via a mevalonate-independent pathway. Proceedings of the National Academy of Sciences, 95, 2100-2104. Retrieved from http://www.pnas.org/10.1073/pnas.95.5.2100
    • (1998) Proceedings of the National Academy of Sciences , vol.95 , pp. 2100-2104
    • Lange, B.M.1    Wildung, M.R.2    McCaskill, D.3    Croteau, R.4
  • 36
    • 12344299758 scopus 로고    scopus 로고
    • Stereochemical studies on the making and unmaking of isopentenyl diphosphate in different biological systems
    • Laupitz, R., Gräwert, T., Rieder, C., Zepeck, F., Bacher, A., Arigoni, D.,., Eisenreich, W. (2004). Stereochemical studies on the making and unmaking of isopentenyl diphosphate in different biological systems. Chemistry & Biodiversity, 1, 1367-1376.
    • (2004) Chemistry & Biodiversity , vol.1 , pp. 1367-1376
    • Laupitz, R.1    Gräwert, T.2    Rieder, C.3    Zepeck, F.4    Bacher, A.5    Arigoni, D.6    Eisenreich, W.7
  • 37
    • 84870249445 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A., Lombardo, F., Dominy, B. W., Feeney, P. J. (2012). Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Advanced Drug Delivery Reviews, 64, 4-17.
    • (2012) Advanced Drug Delivery Reviews , vol.64 , pp. 4-17
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 39
    • 0032478189 scopus 로고    scopus 로고
    • Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis
    • Retrieved from
    • Lois, L. M., Campos, N., Putra, S. R., Danielsen, K., Rohmer, M., Boronat, A. (1998). Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis. Proceedings of the National Academy of Sciences, 95, 2105-2110. Retrieved from http://www.pnas.org/10.1073/pnas.95.5.2105
    • (1998) Proceedings of the National Academy of Sciences , vol.95 , pp. 2105-2110
    • Lois, L.M.1    Campos, N.2    Putra, S.R.3    Danielsen, K.4    Rohmer, M.5    Boronat, A.6
  • 40
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional proles
    • Lüthy, R., Bowie, J. U., Eisenberg, D. (1992). Assessment of protein models with three-dimensional proles. Nature, 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 43
    • 0019404112 scopus 로고
    • 5-[(Hydroxymethyl)-O-pyrophosphoryl]uracil, an intermediate in the biosynthesis of alpha.-putrescinylthymine in deoxyribonucleic acid of bacteriophage.vphi.W-14
    • Maltman, K. L., Neuhard, J., Warren, R. A. J. (1981). 5-[(Hydroxymethyl)-O-pyrophosphoryl]uracil, an intermediate in the biosynthesis of alpha.-putrescinylthymine in deoxyribonucleic acid of bacteriophage.vphi.W-14. Biochemistry, 20, 3586-3591.
    • (1981) Biochemistry , vol.20 , pp. 3586-3591
    • Maltman, K.L.1    Neuhard, J.2    Warren, R.A.J.3
  • 45
    • 79960266042 scopus 로고    scopus 로고
    • Measurement of carbon flux through the MEP pathway for isoprenoid synthesis by 31P-NMR spectroscopy after specific inhibition of 2-C-methyl-d-erythritol 2, 4-cyclodiphosphate reductase. Effect of light and temperature
    • Mongélard, G., Seemann, M., Boisson, A., Rohmer, M., Bligny, R., Rivasseau, C. (2011). Measurement of carbon flux through the MEP pathway for isoprenoid synthesis by 31P-NMR spectroscopy after specific inhibition of 2-C-methyl-d-erythritol 2, 4-cyclodiphosphate reductase. Effect of light and temperature. Plant, Cell & Environment, 34, 1241-1247.
    • (2011) Plant, Cell & Environment , vol.34 , pp. 1241-1247
    • Mongélard, G.1    Seemann, M.2    Boisson, A.3    Rohmer, M.4    Bligny, R.5    Rivasseau, C.6
  • 46
    • 0024293191 scopus 로고
    • Isopentenyl-diphosphate isomerase: Inactivation of the enzyme with active-site-directed irreversible inhibitors and transition state analogs
    • Muehlbacher, M., Poulter, C. D. (1988). Isopentenyl-diphosphate isomerase: Inactivation of the enzyme with active-site-directed irreversible inhibitors and transition state analogs. Biochemistry, 27, 7315-7328.
    • (1988) Biochemistry , vol.27 , pp. 7315-7328
    • Muehlbacher, M.1    Poulter, C.D.2
  • 47
    • 71749113661 scopus 로고    scopus 로고
    • IspG converts an epoxide substrate analogue to (E)-4-hydroxy-3-methylbut-2-enyl diphosphate: Implications for IspG catalysis in isoprenoid biosynthesis
    • Nyland II, R. L., II, Xiao, Y., Liu, P., Freel Meyers, C. L. (2009). IspG converts an epoxide substrate analogue to (E)-4-hydroxy-3-methylbut-2-enyl diphosphate: Implications for IspG catalysis in isoprenoid biosynthesis. Journal of the American Chemical Society, 131, 17734-17735.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 17734-17735
    • Nyland, I.I.R.L.1    Xiao, I.I.Y.2    Liu, P.3    Freel Meyers, C.L.4
  • 48
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M., Rahman, A. (1981). Polymorphic transitions in single crystals: A new molecular dynamics method. Journal of Applied physics, 52, 7182-7190.
    • (1981) Journal of Applied Physics , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 50
    • 0030598343 scopus 로고    scopus 로고
    • Deviations from standard atomic volumes as a quality measure for protein crystal structures
    • Pontius, J., Richelle, J., Wodak, S. J. (1996). Deviations from standard atomic volumes as a quality measure for protein crystal structures. Journal of Molecular Biology, 264, 121-136.
    • (1996) Journal of Molecular Biology , vol.264 , pp. 121-136
    • Pontius, J.1    Richelle, J.2    Wodak, S.J.3
  • 52
    • 33646463290 scopus 로고    scopus 로고
    • Bifunctional inhibitors of mevalonate kinase and mevalonate 5-diphosphate decarboxylase
    • Qiu, Y., Li, D. (2006). Bifunctional inhibitors of mevalonate kinase and mevalonate 5-diphosphate decarboxylase. Organic Letters, 8, 1013-1016.
    • (2006) Organic Letters , vol.8 , pp. 1013-1016
    • Qiu, Y.1    Li, D.2
  • 53
    • 0014381393 scopus 로고
    • Conformation of polypeptides and proteins
    • In C. B. Annsen, M. L. Anson, J. T. Edsall, & F. New York, NY: Elsevier M. Richards. (Eds)
    • Ramachandran, G. N., Sasisekharan, V. (1968). Conformation of polypeptides and proteins. In C. B. Annsen, M. L. Anson, J. T. Edsall, & F. M. Richards. (Eds.), Advances in protein chemistry (pp. 283-437). New York, NY: Elsevier.
    • (1968) Advances in Protein Chemistry , pp. 283-437
    • Ramachandran, G.N.1    Sasisekharan, V.2
  • 54
  • 56
    • 0033213706 scopus 로고    scopus 로고
    • The discovery of a mevalonate-independent pathway for isoprenoid biosynthesis in bacteria, algae and higher plants†
    • Rohmer, M. (1999). The discovery of a mevalonate-independent pathway for isoprenoid biosynthesis in bacteria, algae and higher plants†. Natural Product Reports, 16, 565-574.
    • (1999) Natural Product Reports , vol.16 , pp. 565-574
    • Rohmer, M.1
  • 57
    • 42049122363 scopus 로고    scopus 로고
    • Structure-based drug design targeting biosynthesis of isoprenoids: A crystallographic state of the art of the involved enzymes
    • Ruyck, J. D., Wouters, J. (2008). Structure-based drug design targeting biosynthesis of isoprenoids: A crystallographic state of the art of the involved enzymes. Current Protein & Peptide Science, 9, 117-137.
    • (2008) Current Protein & Peptide Science , vol.9 , pp. 117-137
    • Ruyck, J.D.1    Wouters, J.2
  • 58
    • 0030846307 scopus 로고    scopus 로고
    • Creating isoprenoid diversity
    • Sacchettini, J. C., Poulter, C. D. (1997). Creating isoprenoid diversity. Science, 277, 1788-1789.
    • (1997) Science , vol.277 , pp. 1788-1789
    • Sacchettini, J.C.1    Poulter, C.D.2
  • 59
    • 70349404627 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis via the MEP pathway: In vivo Mossbauer spectroscopy identifies a [4Fe-4S]2+ center with unusual coordination sphere in the LytB protein
    • Seemann, M., Janthawornpong, K., Schweizer, J., Bottger, L. H., Janoschka, A., Ahrens-Botzong, A.,., Rohmer, M. (2009). Isoprenoid biosynthesis via the MEP pathway: in vivo Mossbauer spectroscopy identifies a [4Fe-4S]2+ center with unusual coordination sphere in the LytB protein. Journal of the American Chemical Society, 131, 13184-13185.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 13184-13185
    • Seemann, M.1    Janthawornpong, K.2    Schweizer, J.3    Bottger, L.H.4    Janoschka, A.5    Ahrens-Botzong, A.6    Rohmer, M.7
  • 60
    • 34547697909 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis via the methylerythritol phosphate pathway: GcpE and LytB, two novel iron-sulphur proteins
    • Seemann, M., Rohmer, M. (2007). Isoprenoid biosynthesis via the methylerythritol phosphate pathway: GcpE and LytB, two novel iron-sulphur proteins. Comptes Rendus Chimie, 10, 748-755.
    • (2007) Comptes Rendus Chimie , vol.10 , pp. 748-755
    • Seemann, M.1    Rohmer, M.2
  • 62
    • 0030696041 scopus 로고    scopus 로고
    • Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol
    • Retrieved from
    • Sprenger, G. A., Schörken, U., Wiegert, T., Grolle, S., De Graaf, A. A., Taylor, S. V.,., Sahm, H. (1997). Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proceedings of the National Academy of Sciences, 94, 12857-12862. Retrieved from http://www.pnas.org/10.1073/pnas.94.24.12857
    • (1997) Proceedings of the National Academy of Sciences , vol.94 , pp. 12857-12862
    • Sprenger, G.A.1    Schörken, U.2    Wiegert, T.3    Grolle, S.4    De Graaf, A.A.5    Taylor, S.V.6    Sahm, H.7
  • 63
    • 0029099223 scopus 로고
    • Regulation of immunity to malaria: Valuable lessons learned from murine models
    • Taylor-Robinson, A. W. (1995). Regulation of immunity to malaria: Valuable lessons learned from murine models. Parasitology Today, 11, 334-342.
    • (1995) Parasitology Today , vol.11 , pp. 334-342
    • Taylor-Robinson, A.W.1
  • 64
    • 0037606114 scopus 로고    scopus 로고
    • Ligand-Info, searching for similar small compounds using index profiles
    • von Grotthuss, M., Pas, J., Rychlewski, L. (2003). Ligand-Info, searching for similar small compounds using index profiles. Bioinformatics, 19, 1041-1042.
    • (2003) Bioinformatics , vol.19 , pp. 1041-1042
    • Von Grotthuss, M.1    Pas, J.2    Rychlewski, L.3
  • 65
    • 77954921896 scopus 로고    scopus 로고
    • Organometallic mechanism of action and inhibition of the 4Fe-4S isoprenoid biosynthesis protein GcpE (IspG)
    • Wang, W., Li, J., Wang, K., Huang, C., Zhang, Y., Oldfield, E. (2010). Organometallic mechanism of action and inhibition of the 4Fe-4S isoprenoid biosynthesis protein GcpE (IspG). Proceedings of the National Academy of Sciences, 107, 11189-11193.
    • (2010) Proceedings of the National Academy of Sciences , vol.107 , pp. 11189-11193
    • Wang, W.1    Li, J.2    Wang, K.3    Huang, C.4    Zhang, Y.5    Oldfield, E.6
  • 66
    • 79955406738 scopus 로고    scopus 로고
    • Pyridine inhibitor binding to the 4Fe-4S protein A. Aeolicus IspH (LytB): A HYSCORE Investigation
    • Wang, W., Li, J., Wang, K., Smirnova, T. I., Oldfield, E. (2011). Pyridine inhibitor binding to the 4Fe-4S protein A. aeolicus IspH (LytB): A HYSCORE Investigation. Journal of the American Chemical Society, 133, 6525-6528.
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 6525-6528
    • Wang, W.1    Li, J.2    Wang, K.3    Smirnova, T.I.4    Oldfield, E.5
  • 69
    • 58149092426 scopus 로고    scopus 로고
    • Conformational dynamics of the flexible catalytic loop in mycobacterium tuberculosis 1-deoxy-d-xylulose 5-phosphate reductoisomerase
    • Williams, S. L., Andrew McCammon, J. (2009). Conformational dynamics of the flexible catalytic loop in mycobacterium tuberculosis 1-deoxy-d-xylulose 5-phosphate reductoisomerase. Chemical Biology & Drug Design, 73, 26-38.
    • (2009) Chemical Biology & Drug Design , vol.73 , pp. 26-38
    • Williams, S.L.1    Andrew McCammon, J.2
  • 71
    • 0346458808 scopus 로고    scopus 로고
    • Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor
    • Wouters, J., Oudjama, Y., Stalon, V., Droogmans, L., Poulter, C. D. (2004). Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor. Proteins: Structure, Function, and Bioinformatics, 54, 216-221.
    • (2004) Proteins: Structure, Function, and Bioinformatics , vol.54 , pp. 216-221
    • Wouters, J.1    Oudjama, Y.2    Stalon, V.3    Droogmans, L.4    Poulter, C.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.