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Volumn 8, Issue 10, 2013, Pages

Role of Key Salt Bridges in Thermostability of G. thermodenitrificans EstGtA2: Distinctive Patterns within the New Bacterial Lipolytic Enzyme Family XV

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL ENZYME; BACTERIAL PROTEIN; BRIDGED PEPTIDE; HISTIDINE; LIPOLYTIC ENZYME FAMILY 15; PROTEIN ESTGTA2; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84885104535     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0076675     Document Type: Article
Times cited : (42)

References (56)
  • 1
    • 0026540411 scopus 로고
    • The alpha/beta hydrolase fold
    • doi:10.1093/protein/5.3.197
    • Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, et al. (1992) The alpha/beta hydrolase fold. Protein Eng 5(3):: 197-211. doi:10.1093/protein/5.3.197. PubMed: 1409539.
    • (1992) Protein Eng , vol.5 , pp. 197-211
    • Ollis, D.L.1    Cheah, E.2    Cygler, M.3    Dijkstra, B.4    Frolow, F.5
  • 2
    • 0032784276 scopus 로고    scopus 로고
    • α/β hydrolase fold enzymes: the family keeps growing
    • doi:10.1016/S0959-440X(99)00037-8
    • Nardini M, Dijkstra BW, (1999) α/β hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol 9: 732-737. doi:10.1016/S0959-440X(99)00037-8. PubMed: 10607665.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 3
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • doi:10.1042/0264-6021:3430177
    • Arpigny JL, Jaeger K-E, (1999) Bacterial lipolytic enzymes: classification and properties. Biochem J 343: 177-183. doi:10.1042/0264-6021:3430177. PubMed: 10493927.
    • (1999) Biochem J , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.-E.2
  • 4
    • 84875966177 scopus 로고    scopus 로고
    • A novel alkaliphilic Bacillus esterase belongs to the 13th bacterial lipolytic enzyme family
    • doi:10.1371/journal.pone.0060645
    • Rao L, Xue Y, Zheng Y, Lu JR, Ma Y, (2013) A novel alkaliphilic Bacillus esterase belongs to the 13th bacterial lipolytic enzyme family. PLOS ONE 8(4):: e60645. doi:10.1371/journal.pone.0060645. PubMed: 23577139.
    • (2013) PLOS ONE , vol.8
    • Rao, L.1    Xue, Y.2    Zheng, Y.3    Lu, J.R.4    Ma, Y.5
  • 5
    • 65549128344 scopus 로고    scopus 로고
    • Characterization of a novel carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family
    • doi:10.1128/JB.01060-08
    • Montoro-García S, Martínez-Martínez I, Navarro-Fernández J, Takami H, García-Carmona F, et al. (2009) Characterization of a novel carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family. J Bacteriol 191(9):: 3076-3085. doi:10.1128/JB.01060-08. PubMed: 19304850.
    • (2009) J Bacteriol , vol.191 , pp. 3076-3085
    • Montoro-García, S.1    Martínez-Martínez, I.2    Navarro-Fernández, J.3    Takami, H.4    García-Carmona, F.5
  • 6
    • 4344637340 scopus 로고    scopus 로고
    • Covalent reaction intermediate in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30
    • doi:10.1016/j.jmb.2004.06.069
    • Liu P, Wang YF, Ewis HE, Abdelal AT, Lu CD, et al. (2004) Covalent reaction intermediate in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30. J Mol Biol 342: 551-561. doi:10.1016/j.jmb.2004.06.069. PubMed: 15327954.
    • (2004) J Mol Biol , vol.342 , pp. 551-561
    • Liu, P.1    Wang, Y.F.2    Ewis, H.E.3    Abdelal, A.T.4    Lu, C.D.5
  • 7
    • 77956442168 scopus 로고    scopus 로고
    • A novel thermostable carboxylesterase from Geobacillus thermodenitrificans: Evidence for a new carboxylesterase family
    • doi:10.1093/jb/mvq064
    • Charbonneau DM, Meddeb-Mouelhi F, Beauregard M, (2010) A novel thermostable carboxylesterase from Geobacillus thermodenitrificans: Evidence for a new carboxylesterase family. J Biochem 148: 299-308. doi:10.1093/jb/mvq064. PubMed: 20587647.
    • (2010) J Biochem , vol.148 , pp. 299-308
    • Charbonneau, D.M.1    Meddeb-Mouelhi, F.2    Beauregard, M.3
  • 8
    • 84868087357 scopus 로고    scopus 로고
    • The Metagenome-Derived Enzymes LipS and LipT Increase the Diversity of Known Lipases
    • doi:10.1371/journal.pone.0047665
    • Chow J, Kovacic F, Dall Antonia Y, Krauss U, Fersini F, et al. (2012) The Metagenome-Derived Enzymes LipS and LipT Increase the Diversity of Known Lipases. PLOS ONE 7(10):: e47665. doi:10.1371/journal.pone.0047665. PubMed: 23112831.
    • (2012) PLOS ONE , vol.7
    • Chow, J.1    Kovacic, F.2    Dall Antonia, Y.3    Krauss, U.4    Fersini, F.5
  • 9
    • 0037246592 scopus 로고    scopus 로고
    • The lipase engineering database: a navigation and analysis tool for protein families
    • doi:10.1093/nar/gkg015
    • Fischer M, Pleiss J, (2003) The lipase engineering database: a navigation and analysis tool for protein families. Nucleic Acids Res 31: 319-321. doi:10.1093/nar/gkg015. PubMed: 12520012.
    • (2003) Nucleic Acids Res , vol.31 , pp. 319-321
    • Fischer, M.1    Pleiss, J.2
  • 10
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: classification, properties and application in biocatalysis
    • doi:10.1111/j.1574-6976.2002.tb00599.x
    • Bornscheuer UT, (2002) Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev 26: 73-81. doi:10.1111/j.1574-6976.2002.tb00599.x. PubMed: 12007643.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 11
    • 0032514678 scopus 로고    scopus 로고
    • Protein thermostability above 100 degrees C: a key role for ionic interactions
    • doi:10.1073/pnas.95.21.12300
    • Vetriani C, Maeder DL, Tolliday N, Yip KS, Stillman TJ, et al. (1998) Protein thermostability above 100 degrees C: a key role for ionic interactions. Proc Natl Acad Sci U S A 95: 12300-12305. doi:10.1073/pnas.95.21.12300. PubMed: 9770481.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12300-12305
    • Vetriani, C.1    Maeder, D.L.2    Tolliday, N.3    Yip, K.S.4    Stillman, T.J.5
  • 12
    • 0037041035 scopus 로고    scopus 로고
    • The crystal structure of indoleglycerol -phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges
    • doi:10.1074/jbc.M109517200
    • Knöchel T, Pappenberger A, Jansonius JN, Kirschner K, (2002) The crystal structure of indoleglycerol -phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges. J Biol Chem 277: 8626-8834. doi:10.1074/jbc.M109517200. PubMed: 11741953.
    • (2002) J Biol Chem , vol.277 , pp. 8626-8834
    • Knöchel, T.1    Pappenberger, A.2    Jansonius, J.N.3    Kirschner, K.4
  • 13
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • doi:10.1074/jbc.M401865200
    • Bae E, Phillips GN, (2004) Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J Biol Chem 279: 28202-28208. doi:10.1074/jbc.M401865200. PubMed: 15100224.
    • (2004) J Biol Chem , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips, G.N.2
  • 14
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • doi:10.1093/protein/13.3.179
    • Kumar S, Tsai C-J, Nussinov R, (2000) Factors enhancing protein thermostability. Prot Eng 13: 179-191. doi:10.1093/protein/13.3.179. PubMed: 10775659.
    • (2000) Prot Eng , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.-J.2    Nussinov, R.3
  • 15
    • 0034673153 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability
    • doi:10.1021/bi992257j
    • Strop P, Mayo SL, (2000) Contribution of surface salt bridges to protein stability. Biochemistry 39(6):: 1251-1255. doi:10.1021/bi992257j. PubMed: 10684603.
    • (2000) Biochemistry , vol.39 , pp. 1251-1255
    • Strop, P.1    Mayo, S.L.2
  • 16
    • 0034633994 scopus 로고    scopus 로고
    • Contribution of salt bridges near the surface of a protein to the conformational stability
    • doi:10.1021/bi000849s
    • Takano K, Tsuchimori K, Yamagata Y, Yutani K, (2000) Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry 39(40):: 12375-12381. doi:10.1021/bi000849s. PubMed: 11015217.
    • (2000) Biochemistry , vol.39 , pp. 12375-12381
    • Takano, K.1    Tsuchimori, K.2    Yamagata, Y.3    Yutani, K.4
  • 17
    • 0037432563 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability: guidelines for protein engineering
    • Makhatadze GI, Loladze VV, Ermolenko DN, Chen X, Thomas ST, (2003) Contribution of surface salt bridges to protein stability: guidelines for protein engineering. J Mol Biol 237(5):: 1135-1148. PubMed: 12662936.
    • (2003) J Mol Biol , vol.237 , pp. 1135-1148
    • Makhatadze, G.I.1    Loladze, V.V.2    Ermolenko, D.N.3    Chen, X.4    Thomas, S.T.5
  • 18
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridges stability in monomeric proteins
    • doi:10.1006/jmbi.1999.3218
    • Kumar S, Nussinov R, (1999) Salt bridges stability in monomeric proteins. J Mol Biol 293(5):: 1241-1255. doi:10.1006/jmbi.1999.3218. PubMed: 10547298.
    • (1999) J Mol Biol , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 19
    • 0024318970 scopus 로고
    • pH-dependence of the reversible and irreversible thermal denaturation of g interferon
    • doi:10.1021/bi00442a005
    • Mulkerrin MG, Wetzel R, (1989) pH-dependence of the reversible and irreversible thermal denaturation of g interferon. Biochem 28: 6556-6561. doi:10.1021/bi00442a005.
    • (1989) Biochem , vol.28 , pp. 6556-6561
    • Mulkerrin, M.G.1    Wetzel, R.2
  • 20
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • doi:10.1126/science.694508
    • Perutz MF, (1978) Electrostatic effects in proteins. Science 201: 1187-1191. doi:10.1126/science.694508. PubMed: 694508.
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.F.1
  • 21
    • 17644365489 scopus 로고    scopus 로고
    • Structural features of thermozymes
    • doi:10.1016/j.biotechadv.2005.01.002
    • Li WF, Zhou XX, Lu P, (2005) Structural features of thermozymes. Biotechnol Adv. 23: 271-281. doi:10.1016/j.biotechadv.2005.01.002. PubMed: 15848038.
    • (2005) Biotechnol Adv , vol.23 , pp. 271-281
    • Li, W.F.1    Zhou, X.X.2    Lu, P.3
  • 22
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanism for thermostability
    • doi:10.1128/MMBR.65.1.1-43.2001
    • Vieille C, Zeikus GJ, (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanism for thermostability. Microbiol Mol Biol Rev 65(1):: 1-43. doi:10.1128/MMBR.65.1.1-43.2001. PubMed: 11238984.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 23
    • 28244464396 scopus 로고    scopus 로고
    • Conversion of a carboxylesterase into a triacylglycerol lipase by a random mutation
    • doi:10.1002/anie.200502461
    • Reyes-Duarte D, Polaina J, López-Cortés N, Alcalde M, Plou FJ, Elborough K, et al. (2005) Conversion of a carboxylesterase into a triacylglycerol lipase by a random mutation. Angew Chem Int Ed Engl 44(46):: 7553-7557. doi:10.1002/anie.200502461. PubMed: 16254934.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 7553-7557
    • Reyes-Duarte, D.1    Polaina, J.2    López-Cortés, N.3    Alcalde, M.4    Plou, F.J.5    Elborough, K.6
  • 24
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • doi:10.1016/S0006-3495(02)73929-5
    • Kumar S, Nussinov R, (2002) Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys J 83(3):: 1595-1612. doi:10.1016/S0006-3495(02)73929-5. PubMed: 12202384.
    • (2002) Biophys J , vol.83 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 25
    • 44949145248 scopus 로고    scopus 로고
    • Contribution of charged groups to the enthalpic stabilization of the folded states of globular proteins
    • doi:10.1021/jp077024d
    • Dadarlat VM, Post CM, (2008) Contribution of charged groups to the enthalpic stabilization of the folded states of globular proteins. J Phys Chem B 112(19):: 6159-6167. doi:10.1021/jp077024d. PubMed: 18303881.
    • (2008) J Phys Chem B , vol.112 , pp. 6159-6167
    • Dadarlat, V.M.1    Post, C.M.2
  • 26
    • 62649163398 scopus 로고    scopus 로고
    • Defining the role of salt bridges in protein stability
    • doi:10.1007/978-1-59745-367-7_10
    • Jelesarov I, Karshikoff A, (2009) Defining the role of salt bridges in protein stability. Methods Mol Biol 490: 227-260. doi:10.1007/978-1-59745-367-7_10. PubMed: 19157086.
    • (2009) Methods Mol Biol , vol.490 , pp. 227-260
    • Jelesarov, I.1    Karshikoff, A.2
  • 27
    • 79551556876 scopus 로고    scopus 로고
    • Thermostability in endoglucanase is fold-specific
    • doi:10.1186/1472-6807-11-10
    • Yennamalli RM, Rader AJ, Wolt JD, Sen TZ, (2011) Thermostability in endoglucanase is fold-specific. BCM J Struct Biol 11(10). doi:10.1186/1472-6807-11-10.
    • (2011) BCM J Struct Biol , vol.11
    • Yennamalli, R.M.1    Rader, A.J.2    Wolt, J.D.3    Sen, T.Z.4
  • 28
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • doi:10.1002/(SICI)1097-0134(19990515)35:3
    • Johnson WC, (1999) Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins 35(3):: 307-312. doi:10.1002/(SICI)1097-0134(19990515)35:3. PubMed: 10328265.
    • (1999) Proteins , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 29
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structures from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR with an expended reference set
    • doi:10.1006/abio.2000.4880
    • Sreerama N, Woody RW, (2000) Estimation of protein secondary structures from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR with an expended reference set. Anal Biochem 287: 252-260. doi:10.1006/abio.2000.4880. PubMed: 11112271.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 30
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Oxford University Press
    • Pace CN, Shirley BA, Thompson JA, (1989) Measuring the conformational stability of a protein. In: Creighton TE, eds. Protein structure-A practical approach. Oxford University Press. pp. pp. 311-330.
    • (1989) Protein Structure-A Practical Approach , pp. 311-330
    • Creighton, T.E.1
  • 31
    • 84883580751 scopus 로고    scopus 로고
    • BLAST: a more efficient report with usability improvements
    • doi:10.1093/nar/gkt282
    • Boratyn GM, Camacho C, Cooper PS, Coulouris G, Fong A, et al. (2013) BLAST: a more efficient report with usability improvements. Nucleic Acids Res, 41: W29-33. doi:10.1093/nar/gkt282. PubMed: 23609542.
    • (2013) Nucleic Acids Res , vol.41
    • Boratyn, G.M.1    Camacho, C.2    Cooper, P.S.3    Coulouris, G.4    Fong, A.5
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignments through sequence weighting, position-specific gap penalties and weight matrix choice
    • doi:10.1093/nar/22.22.4673
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignments through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22(22):: 4673-4680. doi:10.1093/nar/22.22.4673. PubMed: 7984417.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0032961270 scopus 로고    scopus 로고
    • ESpript: analysis of multiple sequence alignments in PostScript
    • doi:10.1093/bioinformatics/15.4.305
    • Gouet P, Courcelle E, Stuart DI, Métoz F, (1999) ESpript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15(4):: 305-308. doi:10.1093/bioinformatics/15.4.305. PubMed: 10320398.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4
  • 35
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Moldecular Evolutionary Genetics Analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • doi:10.1093/molbev/msr121
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. (2011) MEGA5: Moldecular Evolutionary Genetics Analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28(10):: 2731-2739. doi:10.1093/molbev/msr121. PubMed: 21546353.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5
  • 36
    • 0023375195 scopus 로고
    • The neighbour-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M, (1987) The neighbour-joining method: A new method for reconstructing phylogenetic trees. Mol Biol Evol 4(4):: 406-425. PubMed: 3447015.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 37
    • 0036740806 scopus 로고    scopus 로고
    • ESyPred3D: Prediction of protein structures
    • doi:10.1093/bioinformatics/18.9.1250
    • Lambert C, Léonard N, De Bolle X, Depiereux E, (2002) ESyPred3D: Prediction of protein structures. Bioinformatics 18: 1250-1256. doi:10.1093/bioinformatics/18.9.1250. PubMed: 12217917.
    • (2002) Bioinformatics , vol.18 , pp. 1250-1256
    • Lambert, C.1    Léonard, N.2    De Bolle, X.3    Depiereux, E.4
  • 38
    • 0000243829 scopus 로고
    • PROCHECK - a program to check the stereochemical quality of protein structures
    • doi:10.1107/S0021889892009944
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, (1993) PROCHECK- a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283-291. doi:10.1107/S0021889892009944.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 39
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling
    • doi:10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201. doi:10.1093/bioinformatics/bti770. PubMed: 16301204.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 40
    • 70450224038 scopus 로고    scopus 로고
    • ESBRI: A web served for evaluating salt bridges in proteins
    • Constantini S, Colonna G, Facchiano AM, (2008) ESBRI: A web served for evaluating salt bridges in proteins. Bioinformation 3(2):: 137-138.
    • (2008) Bioinformation , vol.3 , pp. 137-138
    • Constantini, S.1    Colonna, G.2    Facchiano, A.M.3
  • 41
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • doi:10.1002/prot.20660
    • Li H, Robertson AD, Jensen JH, (2005) Very fast empirical prediction and rationalization of protein pKa values. PROTEINS 61: 704-721. doi:10.1002/prot.20660. PubMed: 16231289.
    • (2005) PROTEINS , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 42
    • 0035046039 scopus 로고    scopus 로고
    • Monoacylglycerol lipase from moderately thermophilic Bacillus sp. Strain H-257: Molecular cloning, sequencing and expression in Escherichia coli of the gene
    • Kitaura S, Suzuki K, Imamura S, (2001) Monoacylglycerol lipase from moderately thermophilic Bacillus sp. Strain H-257: Molecular cloning, sequencing and expression in Escherichia coli of the gene. J Biochem, 129: 397-402. PubMed: 11226879.
    • (2001) J Biochem , vol.129 , pp. 397-402
    • Kitaura, S.1    Suzuki, K.2    Imamura, S.3
  • 43
    • 0034108930 scopus 로고    scopus 로고
    • Purification and characterization of a monoacylglycerol lipase from the moderately thermophilic Bacillus sp. H-257
    • Imamura S, Kitaura S, (2000) Purification and characterization of a monoacylglycerol lipase from the moderately thermophilic Bacillus sp. H-257. J Biochem pp. 419-425.
    • (2000) J Biochem , pp. 419-425
    • Imamura, S.1    Kitaura, S.2
  • 44
    • 84860826225 scopus 로고    scopus 로고
    • The structure of monoacylglycerol lipase from Bacillus sp H-257 reveals unexpected conservation of the cap architecture between bacterial and human enzymes
    • Rengachari S, Bezerra GA, Roegler-Berket L, Gruber CC, Sturm C, et al. (2012) The structure of monoacylglycerol lipase from Bacillus sp H-257 reveals unexpected conservation of the cap architecture between bacterial and human enzymes. Biochim Biophys Acta: pp. 1012-1021.
    • (2012) Biochim Biophys Acta , pp. 1012-1021
    • Rengachari, S.1    Bezerra, G.A.2    Roegler-Berket, L.3    Gruber, C.C.4    Sturm, C.5
  • 45
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of tyrosyl-tRNA synthetase (Bacillus starothermophilus)
    • Carter PJ, Winter G, Wilkinson AJ, Fersht AR, (1984) The use of double mutants to detect structural changes in the active site of tyrosyl-tRNA synthetase (Bacillus starothermophilus). Cell 3: 835-840.
    • (1984) Cell , vol.3 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 46
    • 0035358803 scopus 로고    scopus 로고
    • Combinatorial alanine-scanning
    • doi:10.1016/S1367-5931(00)00206-4
    • Morrison KL, Weiss GA, (2001) Combinatorial alanine-scanning. Curr Opin Struct Biol 5: 302-307. doi:10.1016/S1367-5931(00)00206-4. PubMed: 11479122.
    • (2001) Curr Opin Struct Biol , vol.5 , pp. 302-307
    • Morrison, K.L.1    Weiss, G.A.2
  • 47
    • 84860352363 scopus 로고    scopus 로고
    • Highly conserved salt bridge stabilizes rigid signal patch at extracellular loop critical for surface expression of acid-sensing ion channels
    • doi:10.1074/jbc.M111.334250
    • Yang Y, Yu Y, Cheng J, Liu Y, Liu D-S, et al. (2012) Highly conserved salt bridge stabilizes rigid signal patch at extracellular loop critical for surface expression of acid-sensing ion channels. J Biol Chem 287(18):: 14443-14445. doi:10.1074/jbc.M111.334250. PubMed: 22399291.
    • (2012) J Biol Chem , vol.287 , pp. 14443-14445
    • Yang, Y.1    Yu, Y.2    Cheng, J.3    Liu, Y.4    Liu, D.-S.5
  • 48
    • 84856232223 scopus 로고    scopus 로고
    • A conserved Glu-Arg salt bridge connects coevolved motifs that define the eukaryotic kinase fold
    • doi:10.1016/j.jmb.2011.11.035
    • Yang J, Wu J, Steichen JM, Kornev AP, Deal MS, et al. (2012) A conserved Glu-Arg salt bridge connects coevolved motifs that define the eukaryotic kinase fold. J Mol Biol 415(4):: 666-679. doi:10.1016/j.jmb.2011.11.035. PubMed: 22138346.
    • (2012) J Mol Biol , vol.415 , pp. 666-679
    • Yang, J.1    Wu, J.2    Steichen, J.M.3    Kornev, A.P.4    Deal, M.S.5
  • 49
    • 0028485627 scopus 로고
    • Protein stability effects of a complete set of alanine substitutions in Arc repressor
    • doi:10.1038/nsb0894-518
    • Milla ME, Brown BM, Sauer RT, (1994) Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nat Struct Biol 1(8):: 518-523. doi:10.1038/nsb0894-518. PubMed: 7664079.
    • (1994) Nat Struct Biol , vol.1 , pp. 518-523
    • Milla, M.E.1    Brown, B.M.2    Sauer, R.T.3
  • 50
    • 0033514919 scopus 로고    scopus 로고
    • Tolerance of Arc repressor to multiple-alanine substitutions
    • Brown BM, Sauer RT, (1998) Tolerance of Arc repressor to multiple-alanine substitutions. Proc Natl Acad Sci U S A 96: 1983-1988. PubMed: 10051581.
    • (1998) Proc Natl Acad Sci U S A , vol.96 , pp. 1983-1988
    • Brown, B.M.1    Sauer, R.T.2
  • 51
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity
    • doi:10.1038/nsb0295-122
    • Waldburger CD, Schildbach JF, Sauer RT, (1995) Are buried salt bridges important for protein stability and conformational specificity. Nat Struct Biol 2: 122-128. doi:10.1038/nsb0295-122. PubMed: 7749916.
    • (1995) Nat Struct Biol , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 52
    • 0030065958 scopus 로고    scopus 로고
    • Sequence determinant of folding and stability for the P22 Arc repressor
    • Sauer RT, Waldburger CD, Brown BM, Schildbach JF, (1996) Sequence determinant of folding and stability for the P22 Arc repressor. FASEB 10: 42-48.
    • (1996) FASEB , vol.10 , pp. 42-48
    • Sauer, R.T.1    Waldburger, C.D.2    Brown, B.M.3    Schildbach, J.F.4
  • 53
    • 0030067976 scopus 로고    scopus 로고
    • Importance of two buried salt bridges in the stability and folding pathways of Barnase
    • doi:10.1021/bi952930e
    • Tissot AC, Vuilleumier S, Fersht AR, (1996) Importance of two buried salt bridges in the stability and folding pathways of Barnase. Biochemistry 35: 6786-6794. doi:10.1021/bi952930e. PubMed: 8639630.
    • (1996) Biochemistry , vol.35 , pp. 6786-6794
    • Tissot, A.C.1    Vuilleumier, S.2    Fersht, A.R.3
  • 54
    • 0029943662 scopus 로고    scopus 로고
    • A new approach to study of transient protein conformations: The formation of a semiburied salt link in the folding pathway of Barnase
    • doi:10.1021/bi9529317
    • Oliveberg M, Fersht AR, (1996) A new approach to study of transient protein conformations: The formation of a semiburied salt link in the folding pathway of Barnase. Biochemistry 35: 6795-6805. doi:10.1021/bi9529317. PubMed: 8639631.
    • (1996) Biochemistry , vol.35 , pp. 6795-6805
    • Oliveberg, M.1    Fersht, A.R.2
  • 55
    • 79551477576 scopus 로고    scopus 로고
    • Salt bridges: Geometrically specific, designable interactions
    • doi:10.1002/prot.22927
    • Donald JE, Kulp DW, DeGrado DW, (2011) Salt bridges: Geometrically specific, designable interactions. Proteins 79(3):: 898-915. doi:10.1002/prot.22927. PubMed: 21287621.
    • (2011) Proteins , vol.79 , pp. 898-915
    • Donald, J.E.1    Kulp, D.W.2    DeGrado, D.W.3
  • 56
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads
    • doi:10.1016/S0968-0004(01)01918-1
    • Karshikoff A, Ladenstein R, (2001) Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends Biochem Sci 26: 550-556. doi:10.1016/S0968-0004(01)01918-1. PubMed: 11551792.
    • (2001) Trends Biochem Sci , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2


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