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Volumn 28, Issue 7, 2014, Pages 721-734

New insight in the structural features of haloadaptation in α-amylases from halophilic Archaea following homology modeling strategy: Folded and stable conformation maintained through low hydrophobicity and highly negative charged surface

Author keywords

Archaea; Haloadaptation; Halophile; Homology modeling; Stability; Amylase

Indexed keywords

HYDROPHOBICITY; IONIC STRENGTH; MICROORGANISMS;

EID: 84904399997     PISSN: 0920654X     EISSN: 15734951     Source Type: Journal    
DOI: 10.1007/s10822-014-9754-y     Document Type: Article
Times cited : (20)

References (49)
  • 1
    • 0031106921 scopus 로고    scopus 로고
    • Extremophiles
    • Madigan MT, Marrs BL (1997) Extremophiles. Sci Am 276(4):82-87
    • (1997) Sci Am , vol.276 , Issue.4 , pp. 82-87
    • Madigan, M.T.1    Marrs, B.L.2
  • 2
    • 47149088683 scopus 로고    scopus 로고
    • Molecular signature of hypersaline adaptation: Insights from genome and proteome composition of halophilic prokaryotes
    • Paul S, Bag SK, Das S, Harvill ET, Dutta C (2008) Molecular signature of hypersaline adaptation: insights from genome and proteome composition of halophilic prokaryotes. Genome Biol 9(4):R70.
    • (2008) Genome Biol , vol.9 , Issue.4
    • Paul, S.1    Bag, S.K.2    Das, S.3    Harvill, E.T.4    Dutta, C.5
  • 3
    • 0028933771 scopus 로고
    • Life in unusual environments: Progress in understanding the structure and function of enzymes from extreme halophilic bacteria
    • Eisenberg H (1995) Life in unusual environments: progress in understanding the structure and function of enzymes from extreme halophilic bacteria. Arch Biochem Biophys 318(1):1-5
    • (1995) Arch Biochem Biophys , vol.318 , Issue.1 , pp. 1-5
    • Eisenberg, H.1
  • 4
    • 0032518248 scopus 로고    scopus 로고
    • Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii
    • Pieper U, Kapadia G, Mevarech M, Herzberg O (1998) Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii. Structure 6(1):75-88 (Pubitemid 28084401)
    • (1998) Structure , vol.6 , Issue.1 , pp. 75-88
    • Pieper, U.1    Kapadia, G.2    Mevarech, M.3    Herzberg, O.4
  • 5
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • DOI 10.1016/S0959-440X(98)80094-8
    • Jaenicke R, Bohm G (1998) The stability of proteins in extreme environments. Curr Opin Struct Biol 8(6):738-748 (Pubitemid 29004672)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.6 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 7
    • 63849236826 scopus 로고    scopus 로고
    • One-step production of immobilized alpha-amylase in recombinant Escherichia coli
    • Rasiah IA, Rehm BH (2009) One-step production of immobilized alpha-amylase in recombinant Escherichia coli. Appl Environ Microbiol 75(7):2012-2016
    • (2009) Appl Environ Microbiol , vol.75 , Issue.7 , pp. 2012-2016
    • Rasiah, I.A.1    Rehm, B.H.2
  • 8
    • 77952877282 scopus 로고    scopus 로고
    • Engineering of a Bacillus alpha-amylase with improved thermostability and calcium independency
    • Ghollasi M, Khajeh K, Naderi-Manesh H, Ghasemi A (2010) Engineering of a Bacillus alpha-amylase with improved thermostability and calcium independency. Appl Biochem Biotechnol 162(2):444-459
    • (2010) Appl Biochem Biotechnol , vol.162 , Issue.2 , pp. 444-459
    • Ghollasi, M.1    Khajeh, K.2    Naderi-Manesh, H.3    Ghasemi, A.4
  • 9
    • 29244438994 scopus 로고    scopus 로고
    • Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica
    • DOI 10.1007/s00792-005-0471-2
    • Hutcheon GW, Vasisht N, Bolhuis A (2005) Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica. Extremophiles 9(6):487-495 (Pubitemid 41831057)
    • (2005) Extremophiles , vol.9 , Issue.6 , pp. 487-495
    • Hutcheon, G.W.1    Vasisht, N.2    Bolhuis, A.3
  • 10
    • 77949913204 scopus 로고    scopus 로고
    • Alpha-amylase: An ideal representative of thermostable enzymes
    • Prakash O, Jaiswal N (2010) Alpha-amylase: an ideal representative of thermostable enzymes. Appl Biochem Biotechnol 160(8):2401-2414
    • (2010) Appl Biochem Biotechnol , vol.160 , Issue.8 , pp. 2401-2414
    • Prakash, O.1    Jaiswal, N.2
  • 11
    • 0028198814 scopus 로고
    • The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution
    • DOI 10.1021/bi00186a031
    • Qian M, Haser R, Buisson G, Duee E, Payan F (1994) The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution. Biochemistry 33(20):6284-6294 (Pubitemid 24190783)
    • (1994) Biochemistry , vol.33 , Issue.20 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 12
    • 0037187437 scopus 로고    scopus 로고
    • Properties and applications of starch-converting enzymes of the alpha-amylase family
    • DOI 10.1016/S0168-1656(01)00407-2, PII S0168165601004072
    • van der Maarel M, van der Veen B, Uitdehaag J, Leemhuis H, Dijkhuizen L (2002) Properties and applications of starch-converting enzymes of the alpha-amylase family. J Biotechnol 94(2):137-155 (Pubitemid 34127657)
    • (2002) Journal of Biotechnology , vol.94 , Issue.2 , pp. 137-155
    • Van Der, M.M.J.E.C.1    Van Der, V.B.2    Uitdehaag, J.C.M.3    Leemhuis, H.4    Dijkhuizen, L.5
  • 13
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level
    • Aghajari N, Feller G, Gerday C, Haser R (1998) Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level. Structure 6(12):1503-1516 (Pubitemid 29000528)
    • (1998) Structure , vol.6 , Issue.12 , pp. 1503-1516
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 14
    • 0029953633 scopus 로고    scopus 로고
    • Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose
    • Gilles C, Astier JP, Marchis-Mouren G, Cambillau C, Payan F (1996) Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose. Eur J Biochem 238(2):561-569 (Pubitemid 26191164)
    • (1996) European Journal of Biochemistry , vol.238 , Issue.2 , pp. 561-569
    • Gilles, C.1    Astier, J.-P.2    Marchis-Mouren, G.3    Cambillau, C.4    Payan, F.5
  • 15
    • 0000843244 scopus 로고
    • Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: An application of the simulated-annealing method
    • Swift HJ, Brady L, Derewenda ZS, Dodson EJ, Dodson GG, Turkenburg JP, Wilkinson AJ (1991) Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method. Acta Crystallogr B 47(Pt 4):535-544
    • (1991) Acta Crystallogr B , vol.47 , Issue.PART 4 , pp. 535-544
    • Swift, H.J.1    Brady, L.2    Derewenda, Z.S.3    Dodson, E.J.4    Dodson, G.G.5    Turkenburg, J.P.6    Wilkinson, A.J.7
  • 16
    • 0344393458 scopus 로고    scopus 로고
    • Crystal Structure of Bacillus subtilis alpha-Amylase in Complex with Acarbose
    • DOI 10.1128/JB.185.23.6981-6984.2003
    • Kagawa M, Fujimoto Z, Momma M, Takase K, Mizuno H (2003) Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose. J Bacteriol 185(23):6981-6984 (Pubitemid 37444499)
    • (2003) Journal of Bacteriology , vol.185 , Issue.23 , pp. 6981-6984
    • Kagawa, M.1    Fujimoto, Z.2    Momma, M.3    Takase, K.4    Mizuno, H.5
  • 17
    • 0037984394 scopus 로고    scopus 로고
    • Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc
    • DOI 10.1074/jbc.M211339200
    • Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M (2003) Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca, Zn) two-metal center by zinc. J Biol Chem 278(11):9875-9884 (Pubitemid 36800491)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9875-9884
    • Linden, A.1    Mayans, O.2    Meyer-Klaucke, W.3    Antranikian, G.4    Wilmanns, M.5
  • 18
    • 0032563113 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of halophilic proteins
    • DOI 10.1006/jmbi.1998.1904
    • Elcock AH, McCammon JA (1998) Electrostatic contributions to the stability of halophilic proteins. J Mol Biol 280(4):731-748 (Pubitemid 28336377)
    • (1998) Journal of Molecular Biology , vol.280 , Issue.4 , pp. 731-748
    • Elcock, A.H.1    McCammon, J.A.2
  • 19
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • DOI 10.1016/S0301-4622(00)00126-5, PII S0301462200001265
    • Mevarech M, Frolow F, Gloss LM (2000) Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86(2-3):155-164 (Pubitemid 30665604)
    • (2000) Biophysical Chemistry , vol.86 , Issue.2-3 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 20
    • 84055213697 scopus 로고    scopus 로고
    • Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface
    • Siglioccolo A, Paiardini A, Piscitelli M, Pascarella S (2011) Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface. BMC Struct Biol 11:50
    • (2011) BMC Struct Biol , vol.11 , pp. 50
    • Siglioccolo, A.1    Paiardini, A.2    Piscitelli, M.3    Pascarella, S.4
  • 22
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • DOI 10.1093/nar/gkg556
    • Gouet P, Robert X, Courcelle E (2003) ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 31(13):3320-3323 (Pubitemid 37442149)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 23
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234(3):779-815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 24
    • 33646205656 scopus 로고    scopus 로고
    • Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition
    • Sivakumar N, Li N, Tang JW, Patel BK, Swaminathan K (2006) Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition. FEBS Lett 580(11):2646-2652
    • (2006) FEBS Lett , vol.580 , Issue.11 , pp. 2646-2652
    • Sivakumar, N.1    Li, N.2    Tang, J.W.3    Patel, B.K.4    Swaminathan, K.5
  • 25
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • DOI 10.1006/jmbi.1997.1018
    • Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y (1997) The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization. J Mol Biol 269(1):142-153 (Pubitemid 27243627)
    • (1997) Journal of Molecular Biology , vol.269 , Issue.1 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 28
    • 84855186034 scopus 로고    scopus 로고
    • Modelling and bioinformatics analysis of the dimeric structure of house dust mite allergens from families 5 and 21: Der f 5 could dimerize as Der p 5
    • Khemili S, Kwasigroch JM, Hamadouche T, Gilis D (2012) Modelling and bioinformatics analysis of the dimeric structure of house dust mite allergens from families 5 and 21: Der f 5 could dimerize as Der p 5. J Biomol Struct Dyn 29(4):663-675
    • (2012) J Biomol Struct Dyn , vol.29 , Issue.4 , pp. 663-675
    • Khemili, S.1    Kwasigroch, J.M.2    Hamadouche, T.3    Gilis, D.4
  • 29
    • 0034753838 scopus 로고    scopus 로고
    • Identification of homology in protein structure classification
    • DOI 10.1038/nsb1101-953
    • Dietmann S, Holm L (2001) Identification of homology in protein structure classification. Nat Struct Biol 8(11):953-957 (Pubitemid 33032363)
    • (2001) Nature Structural Biology , vol.8 , Issue.11 , pp. 953-957
    • Dietmann, S.1    Holm, L.2
  • 30
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22(12):2577-2637
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 33
    • 84855229636 scopus 로고    scopus 로고
    • PIC: Protein interactions calculator
    • Tina KG, Bhadra R, Srinivasan N (2007) PIC: protein interactions calculator. Nucleic Acids Res 35(Web Server issue):W473-W476
    • (2007) Nucleic Acids Res , vol.35 , Issue.WEB SERVER ISSUE
    • Tina, K.G.1    Bhadra, R.2    Srinivasan, N.3
  • 34
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24(8):1596-1599 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 35
    • 34548286930 scopus 로고    scopus 로고
    • Haloadaptation: Insights from comparative modeling studies of halophilic archaeal DHFRs
    • DOI 10.1016/j.ijbiomac.2007.06.005, PII S014181300700147X
    • Kastritis PL, Papandreou NC, Hamodrakas SJ (2007) Haloadaptation: insights from comparative modeling studies of halophilic archaeal DHFRs. Int J Biol Macromol 41(4):447-453 (Pubitemid 47331635)
    • (2007) International Journal of Biological Macromolecules , vol.41 , Issue.4 , pp. 447-453
    • Kastritis, P.L.1    Papandreou, N.C.2    Hamodrakas, S.J.3
  • 36
    • 84888813652 scopus 로고    scopus 로고
    • Proteinaceous determinants of surface colonization in bacteria: Bacterial adhesion and biofilm formation from a protein secretion perspective
    • Chagnot C, Zorgani MA, Astruc T, Desvaux M (2013) Proteinaceous determinants of surface colonization in bacteria: bacterial adhesion and biofilm formation from a protein secretion perspective. Front Microbiol 4:303
    • (2013) Front Microbiol , vol.4 , pp. 303
    • Chagnot, C.1    Zorgani, M.A.2    Astruc, T.3    Desvaux, M.4
  • 37
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: A semantic awareness issue
    • Desvaux M, Hebraud M, Talon R, Henderson IR (2009) Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol 17(4):139-145
    • (2009) Trends Microbiol , vol.17 , Issue.4 , pp. 139-145
    • Desvaux, M.1    Hebraud, M.2    Talon, R.3    Henderson, I.R.4
  • 38
    • 3042558396 scopus 로고    scopus 로고
    • The general secretory pathway: A general misnomer?
    • DOI 10.1016/j.tim.2004.05.002, PII S0966842X0400112X
    • Desvaux M, Parham NJ, Scott-Tucker A, Henderson IR (2004) The general secretory pathway: a general misnomer? Trends Microbiol 12(7):306-309 (Pubitemid 38829650)
    • (2004) Trends in Microbiology , vol.12 , Issue.7 , pp. 306-309
    • Desvaux, M.1    Parham, N.J.2    Scott-Tucker, A.3    Henderson, I.R.4
  • 39
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • DOI 10.1021/bi962337c
    • Sawaya MR, Kraut J (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36(3):586-603 (Pubitemid 27057006)
    • (1997) Biochemistry , vol.36 , Issue.3 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 41
    • 33344465109 scopus 로고    scopus 로고
    • Amino acid propensities for secondary structures are influenced by the protein structural class
    • DOI 10.1016/j.bbrc.2006.01.159, PII S0006291X06002543
    • Costantini S, Colonna G, Facchiano AM (2006) Amino acid propensities for secondary structures are influenced by the protein structural class. Biochem Biophys Res Commun 342(2):441-451 (Pubitemid 43289012)
    • (2006) Biochemical and Biophysical Research Communications , vol.342 , Issue.2 , pp. 441-451
    • Costantini, S.1    Colonna, G.2    Facchiano, A.M.3
  • 42
    • 12444278965 scopus 로고    scopus 로고
    • Crystal structure of halophilic dodecin: A novel, dodecameric flavin binding protein from Halobacterium salinarum
    • DOI 10.1016/S0969-2126(03)00048-0
    • Bieger B, Essen LO, Oesterhelt D (2003) Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum. Structure 11(4):375-385 (Pubitemid 36419565)
    • (2003) Structure , vol.11 , Issue.4 , pp. 375-385
    • Bieger, B.1    Essen, L.-O.2    Oesterhelt, D.3
  • 44
    • 79955945598 scopus 로고    scopus 로고
    • Protein attributes contribute to halo-stability, bioinformatics approach
    • Ebrahimie E, Ebrahimi M, Sarvestani NR (2011) Protein attributes contribute to halo-stability, bioinformatics approach. Saline Syst 7(1):1
    • (2011) Saline Syst , vol.7 , Issue.1 , pp. 1
    • Ebrahimie, E.1    Ebrahimi, M.2    Sarvestani, N.R.3
  • 45
    • 0028958071 scopus 로고
    • Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium
    • Dym O, Mevarech M, Sussman JL (1995) Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 267(5202):1344-1346
    • (1995) Science , vol.267 , Issue.5202 , pp. 1344-1346
    • Dym, O.1    Mevarech, M.2    Sussman, J.L.3
  • 48
    • 73949105836 scopus 로고    scopus 로고
    • Structural basis for the aminoacid composition of proteins from halophilic archea
    • doi:10.1371/journal.pbio.1000257
    • Tadeo X, Lopez-Mendez B, Trigueros T, Lain A, Castano D, Millet O (2009) Structural basis for the aminoacid composition of proteins from halophilic archea. PLoS Biol 7(12):e1000257. doi:10.1371/journal.pbio.1000257
    • (2009) PLoS Biol , vol.7 , Issue.12
    • Tadeo, X.1    Lopez-Mendez, B.2    Trigueros, T.3    Lain, A.4    Castano, D.5    Millet, O.6
  • 49
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • DOI 10.1016/0022-2836(84)90309-7
    • Eisenberg D, Schwarz E, Komaromy M, Wall R (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 179(1):125-142 (Pubitemid 16223392)
    • (1984) Journal of Molecular Biology , vol.179 , Issue.1 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4


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