메뉴 건너뛰기




Volumn 35, Issue 5, 2017, Pages 1115-1126

A. baumannii histone acetyl transferase Hpa2: optimization of homology modeling, analysis of protein–protein interaction and virtual screening

Author keywords

A. baumannii Hpa2; acetyl CoA; FoldX algorithm; GNAT superfamily; molecular docking

Indexed keywords

ACYLTRANSFERASE; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE GCN5; POLYAMINE; ACETYL COENZYME A; PROTEIN BINDING;

EID: 84978481314     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2016.1172025     Document Type: Article
Times cited : (9)

References (40)
  • 2
    • 0033579559 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily
    • Angus-Hill, M. L., Dutnall, R. N., Tafrov, S. T., Sternglanz, S., & Ramakrishnan, V., (1999). Crystal structure of the histone acetyltransferase Hpa2:A tetrameric member of the Gcn5-related N-acetyltransferase superfamily. Journal of Molecular Biology, 294, 1311–1325.10.1006/jmbi.1999.3338
    • (1999) Journal of Molecular Biology , vol.294 , pp. 1311-1325
    • Angus-Hill, M.L.1    Dutnall, R.N.2    Tafrov, S.T.3    Sternglanz, S.4    Ramakrishnan, V.5
  • 5
    • 79958227569 scopus 로고    scopus 로고
    • The ecology, biology and pathogenesis of Acinetobacter spp.: An overview
    • Doughari, H. J., Alois, P. N., Human, I. S., & Benad, S., (2011). The ecology, biology and pathogenesis of Acinetobacter spp.:An overview. Microbes and Environments, 26, 101–112.10.1264/jsme2.ME10179
    • (2011) Microbes and Environments , vol.26 , pp. 101-112
    • Doughari, H.J.1    Alois, P.N.2    Human, I.S.3    Benad, S.4
  • 6
    • 0032555689 scopus 로고    scopus 로고
    • Structure of the histone acetyltransferase Hat1: A paradigm for the GCN5-related N-acetyl transferase superfamily
    • Dutnall, R. N., Tafrov, S. T., Sternglanz, R., & Ramakrishnan, V., (1998). Structure of the histone acetyltransferase Hat1:A paradigm for the GCN5-related N-acetyl transferase superfamily. Cell, 94, 427–438.10.1016/S0092-8674(00)81584-6
    • (1998) Cell , vol.94 , pp. 427-438
    • Dutnall, R.N.1    Tafrov, S.T.2    Sternglanz, R.3    Ramakrishnan, V.4
  • 7
    • 33144460009 scopus 로고    scopus 로고
    • The epidemiology and control of Acinetobacter baumannii in health care facilities
    • Fournier, P. E., & Richet, H., (2006). The epidemiology and control of Acinetobacter baumannii in health care facilities. Clinical Infectious Diseases, 42, 692–699.10.1086/500202
    • (2006) Clinical Infectious Diseases , vol.42 , pp. 692-699
    • Fournier, P.E.1    Richet, H.2
  • 8
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D. I., & Metoz, F., (1999). ESPript:Multiple sequence alignments in PostScript. Bioinformatics, 15, 305–308.10.1093/bioinformatics/15.4.305
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 9
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • Guerois, R., Nielsen, J. E., & Serrano, L., (2002). Predicting changes in the stability of proteins and protein complexes:A study of more than 1000 mutations. Journal of Molecular Biology, 320, 369–387.10.1016/S0022-2836(02)00442-4
    • (2002) Journal of Molecular Biology , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 10
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative protein modeling
    • Guex, N., & Peitsch, M. C., (1997). SWISS-MODEL and the Swiss-Pdb viewer:An environment for comparative protein modeling. Electrophoresis, 18, 2714–2723.10.1002/(ISSN)1522-2683
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 11
    • 0037474532 scopus 로고    scopus 로고
    • Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme a reveals the mechanism for β-lactam acetylation
    • He, H., Ding, Y., Bartlam, M., Sun, F., Le, Y., Qin, X., Tang, H., … Rao, Z., (2003). Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme a reveals the mechanism for β-lactam acetylation. Journal of Molecular Biology, 325, 1019–1030.10.1016/S0022-2836(02)01284-6
    • (2003) Journal of Molecular Biology , vol.325 , pp. 1019-1030
    • He, H.1    Ding, Y.2    Bartlam, M.3    Sun, F.4    Le, Y.5    Qin, X.6    Tang, H.7    Rao, Z.8
  • 12
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA
    • Hong, L., Schroth, G. P., Matthews, H. R., Yau, P., & Bradbury, E. M., (1993). Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA. Journal of Biological Chemistry, 268, 305–314.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 305-314
    • Hong, L.1    Schroth, G.P.2    Matthews, H.R.3    Yau, P.4    Bradbury, E.M.5
  • 13
    • 0029860794 scopus 로고    scopus 로고
    • Influence of relative humidity and suspending menstrua on survival of Acinetobacter spp. on dry surfaces
    • Jawad, A., Snelling, J., Heritage, A. M., Gascoyne-Binzi, D. M., & Hawkey, P. M., (1996). Influence of relative humidity and suspending menstrua on survival of Acinetobacter spp. on dry surfaces. Journal of Clinical Microbiology, 34, 2881–2887.
    • (1996) Journal of Clinical Microbiology , vol.34 , pp. 2881-2887
    • Jawad, A.1    Snelling, J.2    Heritage, A.M.3    Gascoyne-Binzi, D.M.4    Hawkey, P.M.5
  • 14
    • 27544464928 scopus 로고    scopus 로고
    • Clinical impact and pathogenicity of Acinetobacter
    • Joly-Guillou, M. L., (2005). Clinical impact and pathogenicity of Acinetobacter. Clinical Microbiology and Infection, 11, 868–873.10.1111/j.1469-0691.2005.01227.x
    • (2005) Clinical Microbiology and Infection , vol.11 , pp. 868-873
    • Joly-Guillou, M.L.1
  • 15
    • 29144518532 scopus 로고    scopus 로고
    • The ubiquitin domain superfold: Structure-based sequence alignments and characterization of binding epitopes
    • Kiel, C., & Serrano, L., (2006). The ubiquitin domain superfold:Structure-based sequence alignments and characterization of binding epitopes. Journal of Molecular Biology, 355, 821–844.10.1016/j.jmb.2005.10.010
    • (2006) Journal of Molecular Biology , vol.355 , pp. 821-844
    • Kiel, C.1    Serrano, L.2
  • 16
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo, M. H., & Allis, C. D., (1998). Roles of histone acetyltransferases and deacetylases in gene regulation. BioEssays, 20, 615–626.10.1002/(SICI)1521-1878(199808)20:8<>1.0.CO;2-H
    • (1998) BioEssays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 17
    • 33646462432 scopus 로고    scopus 로고
    • Polyamines induce resistance to cationic peptide, aminoglycoside, and quinolone antibiotics in Pseudomonas aeruginosa PAO1
    • Kwon, D. H., & Lu, C.-D., (2006). Polyamines induce resistance to cationic peptide, aminoglycoside, and quinolone antibiotics in Pseudomonas aeruginosa PAO1. Antimicrobial Agents Chemotherapy, 50, 1615–1622.10.1128/AAC.50.5.1615-1622.2006
    • (2006) Antimicrobial Agents Chemotherapy , vol.50 , pp. 1615-1622
    • Kwon, D.H.1    Lu, C.-D.2
  • 19
    • 0028608018 scopus 로고
    • Histone acetylation: Facts and questions
    • Loidl, P., (1994). Histone acetylation:Facts and questions. Chromosoma, 103, 441–449.10.1007/BF00337382
    • (1994) Chromosoma , vol.103 , pp. 441-449
    • Loidl, P.1
  • 20
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., Bowie, J. U., & Eisenberg, D., (1992). Assessment of protein models with three-dimensional profiles. Nature, 356, 83–85.10.1038/356083a0
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 22
    • 27744481555 scopus 로고    scopus 로고
    • Treatment of multidrug resistant Acinetobacter
    • Murray, C. K., & Hospenthal, D. R., (2005). Treatment of multidrug resistant Acinetobacter. Current Opinion in Infectious Diseases, 18, 502–506.10.1097/01.qco.0000185985.64759.41
    • (2005) Current Opinion in Infectious Diseases , vol.18 , pp. 502-506
    • Murray, C.K.1    Hospenthal, D.R.2
  • 23
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • Norton, V. G., Imai, B. S., Yau, P., & Bradbury, E. M., (1989). Histone acetylation reduces nucleosome core particle linking number change. Cell, 57, 449–457.10.1016/0092-8674(89)90920-3
    • (1989) Cell , vol.57 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 24
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., & Heringa, J., (2000). T-coffee:A novel method for fast and accurate multiple sequence alignment. Journal of Molecular Biology, 302, 205–217.10.1006/jmbi.2000.4042
    • (2000) Journal of Molecular Biology , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 25
    • 33744949446 scopus 로고    scopus 로고
    • The critical roles of polyamines in regulating ColE7 production and restricting ColE7 uptake of the colicin-producing Escherichia coli
    • Pan, Y. H., Liao, C. C., Kuo, C. C., Duan, K. J., Liang, P. H., Yuan, H. S., Hu, S. T., & Chak, K. F., (2006). The critical roles of polyamines in regulating ColE7 production and restricting ColE7 uptake of the colicin-producing Escherichia coli. Journal of Biological Chemistry, 281, 13083–13091.10.1074/jbc.M511365200
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 13083-13091
    • Pan, Y.H.1    Liao, C.C.2    Kuo, C.C.3    Duan, K.J.4    Liang, P.H.5    Yuan, H.S.6    Hu, S.T.7    Chak, K.F.8
  • 26
    • 0003845223 scopus 로고    scopus 로고
    • Version 1.5.0.4), Schrödinger, LLC
    • PyMOL. (2002). Molecular Graphics System (Version 1.5.0.4). Schrödinger, LLC.
    • (2002) Molecular Graphics System
  • 27
    • 79959446944 scopus 로고    scopus 로고
    • Translational recoding as a feedback controller: Systems approaches reveal polyamine-specific effects on the antizyme ribosomal frameshift
    • Rato, C., Amirova, S. R., Bates, D. G., Stansfield, I., & Wallace, H. M., (2011). Translational recoding as a feedback controller:Systems approaches reveal polyamine-specific effects on the antizyme ribosomal frameshift. Nucleic Acids Research, 39, 4587–4597.10.1093/nar/gkq1349
    • (2011) Nucleic Acids Research , vol.39 , pp. 4587-4597
    • Rato, C.1    Amirova, S.R.2    Bates, D.G.3    Stansfield, I.4    Wallace, H.M.5
  • 28
    • 33747589695 scopus 로고    scopus 로고
    • Challenges in identifying new antimicrobial agents effective for treating infections with Acinetobacter baumannii and Pseudomonas aeruginosa
    • Rice, L. B., (2006). Challenges in identifying new antimicrobial agents effective for treating infections with Acinetobacter baumannii and Pseudomonas aeruginosa. Clinical Infectious Diseases, 43, S100–S105.10.1086/504487
    • (2006) Clinical Infectious Diseases , vol.43 , pp. S100-S105
    • Rice, L.B.1
  • 29
    • 84881254916 scopus 로고    scopus 로고
    • Biochemical characterization of Hpa2 and Hpa3-two small closely related acetyltransferases from S. cerevisiae
    • Sampath, V., Liu, B., Tafrov, S., Srinivasan, M., Rieger, R., Chen, E. I., & Sternglanz, R., (2013). Biochemical characterization of Hpa2 and Hpa3-two small closely related acetyltransferases from S. cerevisiae. Journal of Biological Chemistry, 288, 21506–21513.10.1074/jbc.M113.486274
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 21506-21513
    • Sampath, V.1    Liu, B.2    Tafrov, S.3    Srinivasan, M.4    Rieger, R.5    Chen, E.I.6    Sternglanz, R.7
  • 31
    • 40549096043 scopus 로고    scopus 로고
    • A multifaceted role for polyamines in bacterial pathogens
    • Shah, P., & Swiatlo, E., (2008). A multifaceted role for polyamines in bacterial pathogens. Molecular Microbiology, 68, 4–16.10.1111/j.1365-2958.2008.06126.x
    • (2008) Molecular Microbiology , vol.68 , pp. 4-16
    • Shah, P.1    Swiatlo, E.2
  • 32
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D., & Allis, C. D., (2000). The language of covalent histone modifications. Nature, 403, 41–45.10.1038/47412
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 33
    • 1942490112 scopus 로고    scopus 로고
    • A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones
    • Vetting, M. W., Magnet, S., Nieves, E., Roderick, S. L., & Blanchard, J. S., (2004). A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones. Chemistry & Biology, 11, 565–573.
    • (2004) Chemistry & Biology , vol.11 , pp. 565-573
    • Vetting, M.W.1    Magnet, S.2    Nieves, E.3    Roderick, S.L.4    Blanchard, J.S.5
  • 34
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking
    • Vries, S. J. D., Dijk, M. V., & Bonvin, A. M. J. J., (2010). The HADDOCK web server for data-driven biomolecular docking. Nature Protocols, 5, 883–897.10.1038/nprot.2010.32
    • (2010) Nature Protocols , vol.5 , pp. 883-897
    • Vries, S.J.D.1    Dijk, M.V.2    Bonvin, A.M.J.J.3
  • 35
    • 0034602373 scopus 로고    scopus 로고
    • Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model
    • Wang, W., & Kollman, P. A., (2000). Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model. Journal of Molecular Biology, 303, 567–582.10.1006/jmbi.2000.4057
    • (2000) Journal of Molecular Biology , vol.303 , pp. 567-582
    • Wang, W.1    Kollman, P.A.2
  • 36
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • Wiederstein, M., & Sippl, M. J., (2007). ProSA-web:Interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Research, 35, W407–W410.10.1093/nar/gkm290
    • (2007) Nucleic Acids Research , vol.35 , pp. W407-W410
    • Wiederstein, M.1    Sippl, M.J.2
  • 37
    • 0030899291 scopus 로고    scopus 로고
    • Modulation and block of ion channels: A new biology of polyamines
    • Williams, K., (1997). Modulation and block of ion channels:A new biology of polyamines. Cellular Signalling, 9, 1–13.10.1016/S0898-6568(96)00089-7
    • (1997) Cellular Signalling , vol.9 , pp. 1-13
    • Williams, K.1
  • 38
    • 77749264270 scopus 로고    scopus 로고
    • New software and websites for the chemical enterprise
    • Wolf, L. K., (2009). New software and websites for the chemical enterprise. Chemical & Engineering News, 87, 31–33.
    • (2009) Chemical & Engineering News , vol.87 , pp. 31-33
    • Wolf, L.K.1
  • 39
    • 0032555691 scopus 로고    scopus 로고
    • Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase
    • Wolf, E., Vassilev, A., Makino, Y., Sali, A., Nakatani, Y., & Burley, S. K., (1998). Crystal structure of a GCN5-related N-acetyltransferase:Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell, 94, 439–449.10.1016/S0092-8674(00)81585-8
    • (1998) Cell , vol.94 , pp. 439-449
    • Wolf, E.1    Vassilev, A.2    Makino, Y.3    Sali, A.4    Nakatani, Y.5    Burley, S.K.6
  • 40
    • 84895868714 scopus 로고    scopus 로고
    • Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation
    • Worden, E. J., Padovani, C., & Martin, A., (2014). Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation. Nature Structural & Molecular Biology, 21, 220–227.10.1038/nsmb.2771
    • (2014) Nature Structural & Molecular Biology , vol.21 , pp. 220-227
    • Worden, E.J.1    Padovani, C.2    Martin, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.