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Volumn 7, Issue , 2007, Pages

Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ESTERASE; ESTERASE E1; UNCLASSIFIED DRUG; RECOMBINANT PROTEIN;

EID: 34547643363     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-7-47     Document Type: Article
Times cited : (78)

References (38)
  • 1
    • 0036903280 scopus 로고    scopus 로고
    • Methods to increase enantioselectivity of lipases and esterases
    • 10.1016/S0958-1669(02)00350-6. 12482512
    • Methods to increase enantioselectivity of lipases and esterases. UT Bornscheuer, Curr Opin Biotechnol 2002 13 6 543 547 10.1016/S0958-1669(02)00350- 6 12482512
    • (2002) Curr Opin Biotechnol , vol.13 , Issue.6 , pp. 543-547
    • Bornscheuer, U.T.1
  • 2
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • 10.1038/nbt0496-458. 9630920
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. JC Moore FH Arnold, Nat Biotechnol 1996 14 4 458 467 10.1038/nbt0496-458 9630920
    • (1996) Nat Biotechnol , vol.14 , Issue.4 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 3
    • 0141720547 scopus 로고    scopus 로고
    • Regioselective deacetylation of cellulose acetates by acetyl xylan esterases of different CE-families
    • 10.1016/S0168-1656(03)00187-1. 14511913
    • Regioselective deacetylation of cellulose acetates by acetyl xylan esterases of different CE-families. C Altaner B Saake M Tenkanen J Eyzaguirre CB Faulds P Biely L Viikari M Siika-aho J Puls, J Biotechnol 2003 105 1-2 95 104 10.1016/S0168-1656(03)00187-1 14511913
    • (2003) J Biotechnol , vol.105 , Issue.1-2 , pp. 95-104
    • Altaner, C.1    Saake, B.2    Tenkanen, M.3    Eyzaguirre, J.4    Faulds, C.B.5    Biely, P.6    Viikari, L.7    Siika-Aho, M.8    Puls, J.9
  • 4
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • 10.1146/annurev.micro.53.1.315. 10547694
    • Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. KE Jaeger BW Dijkstra MT Reetz, Annu Rev Microbiol 1999 53 315 351 10.1146/annurev.micro.53.1.315 10547694
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 5
    • 13544253396 scopus 로고    scopus 로고
    • New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library
    • 15691936. 10.1128/AEM.71.2.817-825.2005
    • New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library. JK Rhee DG Ahn YG Kim JW Oh, Appl Environ Microbiol 2005 71 2 817 825 15691936 10.1128/AEM.71.2.817-825.2005
    • (2005) Appl Environ Microbiol , vol.71 , Issue.2 , pp. 817-825
    • Rhee, J.K.1    Ahn, D.G.2    Kim, Y.G.3    Oh, J.W.4
  • 6
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: A review
    • 10.1016/S0960-8524(03)00033-6. 12676497
    • Developments in industrially important thermostable enzymes: a review. GD Haki SK Rakshit, Bioresour Technol 2003 89 1 17 34 10.1016/S0960-8524(03)00033- 6 12676497
    • (2003) Bioresour Technol , vol.89 , Issue.1 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 7
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • 10493927. 10.1042/0264-6021:3430177
    • Bacterial lipolytic enzymes: classification and properties. JL Arpigny KE Jaeger, Biochem J 1999 343 Pt 1 177 183 10493927 10.1042/0264-6021:3430177
    • (1999) Biochem J , vol.3431 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 8
    • 33646088728 scopus 로고    scopus 로고
    • Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure
    • 16598011. 10.1128/AEM.72.4.3021-3025.2006
    • Analysis of the thermostability determinants of hyperthermophilic esterase EstE1 based on its predicted three-dimensional structure. JK Rhee DY Kim DG Ahn JH Yun SH Jang HC Shin HS Cho JG Pan JW Oh, Appl Environ Microbiol 2006 72 4 3021 3025 16598011 10.1128/AEM.72.4.3021-3025.2006
    • (2006) Appl Environ Microbiol , vol.72 , Issue.4 , pp. 3021-3025
    • Rhee, J.K.1    Kim, D.Y.2    Ahn, D.G.3    Yun, J.H.4    Jang, S.H.5    Shin, H.C.6    Cho, H.S.7    Pan, J.G.8    Oh, J.W.9
  • 9
    • 0036324633 scopus 로고    scopus 로고
    • Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon
    • 12147492. 10.1128/AEM.68.8.3925-3931.2002
    • Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon. Y Hotta S Ezaki H Atomi T Imanaka, Appl Environ Microbiol 2002 68 8 3925 3931 12147492 10.1128/AEM.68.8.3925-3931.2002
    • (2002) Appl Environ Microbiol , vol.68 , Issue.8 , pp. 3925-3931
    • Hotta, Y.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 10
    • 0033958727 scopus 로고    scopus 로고
    • Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus
    • 10.1006/abbi.1999.1497. 10620337
    • Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus. G Manco E Giosue S D'Auria P Herman G Carrea M Rossi, Arch Biochem Biophys 2000 373 1 182 192 10.1006/abbi.1999.1497 10620337
    • (2000) Arch Biochem Biophys , vol.373 , Issue.1 , pp. 182-192
    • Manco, G.1    Giosue, E.2    D'Auria, S.3    Herman, P.4    Carrea, G.5    Rossi, M.6
  • 11
    • 33646088728 scopus 로고    scopus 로고
    • Analysis of the Thermostability Determinants of Hyperthermophilic Esterase EstE1 Based on Its Predicted Three-Dimensional Structure
    • 16598011. 10.1128/AEM.72.4.3021-3025.2006
    • Analysis of the Thermostability Determinants of Hyperthermophilic Esterase EstE1 Based on Its Predicted Three-Dimensional Structure. JK Rhee DY Kim DG Ahn JH Yun SH Jang HC Shin HS Cho JG Pan JW Oh, Appl Environ Microbiol 2006 72 4 3021 3025 16598011 10.1128/AEM.72.4.3021-3025.2006
    • (2006) Appl Environ Microbiol , vol.72 , Issue.4 , pp. 3021-3025
    • Rhee, J.K.1    Kim, D.Y.2    Ahn, D.G.3    Yun, J.H.4    Jang, S.H.5    Shin, H.C.6    Cho, H.S.7    Pan, J.G.8    Oh, J.W.9
  • 12
    • 0345515997 scopus 로고    scopus 로고
    • The structure of a trimeric archaeal adenylate kinase
    • 10.1006/jmbi.1998.2003. 9733648
    • The structure of a trimeric archaeal adenylate kinase. C Vonrhein H Bonisch G Schafer GE Schulz, J Mol Biol 1998 282 1 167 179 10.1006/jmbi.1998. 2003 9733648
    • (1998) J Mol Biol , vol.282 , Issue.1 , pp. 167-179
    • Vonrhein, C.1    Bonisch, H.2    Schafer, G.3    Schulz, G.E.4
  • 13
    • 0033103161 scopus 로고    scopus 로고
    • X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis
    • 10.1016/S0969-2126(99)80034-3. 10368293
    • X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis. M Singleton M Isupov J Littlechild, Structure 1999 7 3 237 244 10.1016/S0969-2126(99)80034-3 10368293
    • (1999) Structure , vol.7 , Issue.3 , pp. 237-244
    • Singleton, M.1    Isupov, M.2    Littlechild, J.3
  • 14
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • 10.1111/j.1432-1033.1994.tb18623.x. 8119295
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. H Kirino M Aoki M Aoshima Y Hayashi M Ohba A Yamagishi T Wakagi T Oshima, Eur J Biochem 1994 220 1 275 281 10.1111/j.1432-1033.1994. tb18623.x 8119295
    • (1994) Eur J Biochem , vol.220 , Issue.1 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 15
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • 10.1021/bi00066a010. 8471603
    • Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. CA Kelly M Nishiyama Y Ohnishi T Beppu JJ Birktoft, Biochemistry 1993 32 15 3913 3922 10.1021/bi00066a010 8471603
    • (1993) Biochemistry , vol.32 , Issue.15 , pp. 3913-3922
    • Kelly, C.A.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.J.5
  • 16
    • 3543039400 scopus 로고    scopus 로고
    • How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii
    • 10.1074/jbc.M404405200. 15169774
    • How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii. Y Tanaka K Tsumoto Y Yasutake M Umetsu M Yao H Fukada I Tanaka I Kumagai, J Biol Chem 2004 279 31 32957 32967 10.1074/jbc.M404405200 15169774
    • (2004) J Biol Chem , vol.279 , Issue.31 , pp. 32957-32967
    • Tanaka, Y.1    Tsumoto, K.2    Yasutake, Y.3    Umetsu, M.4    Yao, M.5    Fukada, H.6    Tanaka, I.7    Kumagai, I.8
  • 19
    • 0034634338 scopus 로고    scopus 로고
    • A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase
    • 10.1006/jmbi.2000.4195. 11061974
    • A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase. G De Simone S Galdiero G Manco D Lang M Rossi C Pedone, J Mol Biol 2000 303 5 761 771 10.1006/jmbi.2000.4195 11061974
    • (2000) J Mol Biol , vol.303 , Issue.5 , pp. 761-771
    • De Simone, G.1    Galdiero, S.2    Manco, G.3    Lang, D.4    Rossi, M.5    Pedone, C.6
  • 20
    • 0035976710 scopus 로고    scopus 로고
    • The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus
    • 10.1006/jmbi.2001.5152. 11846563
    • The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus. G De Simone V Menchise G Manco L Mandrich N Sorrentino D Lang M Rossi C Pedone, J Mol Biol 2001 314 3 507 518 10.1006/jmbi.2001.5152 11846563
    • (2001) J Mol Biol , vol.314 , Issue.3 , pp. 507-518
    • De Simone, G.1    Menchise, V.2    Manco, G.3    Mandrich, L.4    Sorrentino, N.5    Lang, D.6    Rossi, M.7    Pedone, C.8
  • 22
    • 0033153557 scopus 로고    scopus 로고
    • Of barn owls and bankers: A lush variety of [alpha]/[beta] hydrolases
    • 10.1016/S0969-2126(99)80079-3. 10404588
    • Of barn owls and bankers: a lush variety of [alpha]/[beta] hydrolases. P Heikinheimo A Goldman C Jeffries DL Ollis, Structure 1999 7 6 R141 R146 10.1016/S0969-2126(99)80079-3 10404588
    • (1999) Structure , vol.7 , Issue.6
    • Heikinheimo, P.1    Goldman, A.2    Jeffries, C.3    Ollis, D.L.4
  • 23
    • 0032784276 scopus 로고    scopus 로고
    • [alpha]/[beta] Hydrolase fold enzymes: The family keeps growing
    • 10.1016/S0959-440X(99)00037-8. 10607665
    • [alpha]/[beta] Hydrolase fold enzymes: the family keeps growing. M Nardini BW Dijkstra, Current Opinion in Structural Biology 1999 9 6 732 737 10.1016/S0959-440X(99)00037-8 10607665
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.6 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 24
    • 27844479167 scopus 로고    scopus 로고
    • Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics
    • 10.1074/jbc.M507530200. 16150692
    • Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics. C Duy J Fitter, J Biol Chem 2005 280 45 37360 37365 10.1074/jbc.M507530200 16150692
    • (2005) J Biol Chem , vol.280 , Issue.45 , pp. 37360-37365
    • Duy, C.1    Fitter, J.2
  • 25
    • 0034652006 scopus 로고    scopus 로고
    • The atomic-resolution structure of a novel bacterial esterase
    • 10.1016/S0969-2126(00)00090-3. 10673440
    • The atomic-resolution structure of a novel bacterial esterase. PC Bourne MN Isupov JA Littlechild, Structure 2000 8 2 143 151 10.1016/S0969-2126(00) 00090-3 10673440
    • (2000) Structure , vol.8 , Issue.2 , pp. 143-151
    • Bourne, P.C.1    Isupov, M.N.2    Littlechild, J.A.3
  • 26
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability
    • 10.1006/jmbi.1999.2889. 10390356
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability. MJ Thompson D Eisenberg, Journal of Molecular Biology 1999 290 2 595 604 10.1006/jmbi.1999.2889 10390356
    • (1999) Journal of Molecular Biology , vol.290 , Issue.2 , pp. 595-604
    • Thompson, M.J.1    Eisenberg, D.2
  • 27
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • 11238984. 10.1128/MMBR.65.1.1-43.2001
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. C Vieille GJ Zeikus, Microbiol Mol Biol Rev 2001 65 1 1 43 11238984 10.1128/MMBR.65.1.1-43.2001
    • (2001) Microbiol Mol Biol Rev , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 28
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • 10.1021/bi00483a001. 2207096
    • Dominant forces in protein folding. KA Dill, Biochemistry 1990 29 31 7133 7155 10.1021/bi00483a001 2207096
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 29
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • 10751948
    • Folding and association of oligomeric and multimeric proteins. R Jaenicke H Lilie, Adv Protein Chem 2000 53 329 401 10751948
    • (2000) Adv Protein Chem , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 30
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • 10.1016/S0959-440X(98)80094-8. 9914256
    • The stability of proteins in extreme environments. R Jaenicke G Bohm, Curr Opin Struct Biol 1998 8 6 738 748 10.1016/S0959-440X(98)80094-8 9914256
    • (1998) Curr Opin Struct Biol , vol.8 , Issue.6 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 31
    • 32144449896 scopus 로고    scopus 로고
    • Mean curvature as a major determinant of beta-sheet propensity
    • 10.1093/bioinformatics/bti775. 16287940
    • Mean curvature as a major determinant of beta-sheet propensity. E Koh T Kim HS Cho, Bioinformatics 2006 22 3 297 302 10.1093/bioinformatics/bti775 16287940
    • (2006) Bioinformatics , vol.22 , Issue.3 , pp. 297-302
    • Koh, E.1    Kim, T.2    Cho, H.S.3
  • 32
    • 24644472817 scopus 로고    scopus 로고
    • Physics and evolution of thermophilic adaptation
    • 16120678. 10.1073/pnas.0503890102
    • Physics and evolution of thermophilic adaptation. IN Berezovsky EI Shakhnovich, Proc Natl Acad Sci U S A 2005 102 36 12742 12747 16120678 10.1073/pnas.0503890102
    • (2005) Proc Natl Acad Sci U S a , vol.102 , Issue.36 , pp. 12742-12747
    • Berezovsky, I.N.1    Shakhnovich, E.I.2
  • 33
    • 33646473569 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of EstE1, a new and thermostable esterase cloned from a metagenomic library
    • 10.1107/S1744309106000832. 16511287
    • Crystallization and preliminary X-ray crystallographic analysis of EstE1, a new and thermostable esterase cloned from a metagenomic library. JS Byun JK Rhee DU Kim JW Oh HS Cho, Acta Crystallograph Sect F Struct Biol Cryst Commun 2006 62 Pt 2 145 147 10.1107/S1744309106000832 16511287
    • (2006) Acta Crystallograph Sect F Struct Biol Cryst Commun , vol.62 , Issue.PART 2 , pp. 145-147
    • Byun, J.S.1    Rhee, J.K.2    Kim, D.U.3    Oh, J.W.4    Cho, H.S.5
  • 34
    • 0035210945 scopus 로고    scopus 로고
    • Maximum-likelihood density modification using pattern recognition of structural motifs
    • 10.1107/S0907444901013737. 11717487
    • Maximum-likelihood density modification using pattern recognition of structural motifs. TC Terwilliger, Acta Crystallogr D Biol Crystallogr 2001 57 Pt 12 1755 1762 10.1107/S0907444901013737 11717487
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , Issue.PART 12 , pp. 1755-1762
    • Terwilliger, T.C.1
  • 35
    • 0030931635 scopus 로고    scopus 로고
    • Bayesian correlated MAD phasing
    • 10.1107/S0907444997005398. 15299888
    • Bayesian correlated MAD phasing. TC Terwilliger J Berendzen, Acta Crystallogr D Biol Crystallogr 1997 53 Pt 5 571 579 10.1107/S0907444997005398 15299888
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 5 , pp. 571-579
    • Terwilliger, T.C.1    Berendzen, J.2
  • 36
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 10.1107/S0108767390010224. 2025413
    • Improved methods for building protein models in electron density maps and the location of errors in these models. TA Jones JY Zou SW Cowan Kjeldgaard, Acta Crystallogr A 1991 47 ( Pt 2) 110 119 10.1107/S0108767390010224 2025413
    • (1991) Acta Crystallogr a , vol.472 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Kjeldgaard, W.C.S.3
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • MAMW 10.1107/S0021889892009944
    • PROCHECK: a program to check the stereochemical quality of protein structures. MAMW Laskowski RA Moss DS, Thornton JM, J Appl Crystallogr 1993 26 283 291 10.1107/S0021889892009944
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 38
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 15299374
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994 50 Pt 5 760 763 15299374
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763


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