메뉴 건너뛰기




Volumn 54, Issue 6, 2011, Pages 513-519

Crystal structure of histidine-containing phosphocarrier protein from Thermoanaerobacter tengcongensis MB4 and the implications for thermostability

Author keywords

crystal structure; HPr; salt bridge; Thermoanaerobacter tengcongensis; thermostability

Indexed keywords

BACTERIAL PROTEIN; PHOSPHOCARRIER PROTEIN HPR; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE;

EID: 79959593923     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-011-4182-x     Document Type: Article
Times cited : (3)

References (42)
  • 1
    • 0034884397 scopus 로고    scopus 로고
    • Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China
    • Xue Y, Xu Y, Liu Y, et al. Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China. Int J Syst Evol Microbiol, 2001, 51: 1335-1341.
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 1335-1341
    • Xue, Y.1    Xu, Y.2    Liu, Y.3
  • 2
    • 0036112438 scopus 로고    scopus 로고
    • A complete sequence of the T. tengcongensis genome
    • Bao Q, Tian Y, Li W, et al. A complete sequence of the T. tengcongensis genome. Genome Res, 2002, 12: 689-700.
    • (2002) Genome Res , vol.12 , pp. 689-700
    • Bao, Q.1    Tian, Y.2    Li, W.3
  • 3
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilagyi A, Zavodszky P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure (London, England: 1993), 2000, 8: 493-504.
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 4
    • 0031564613 scopus 로고    scopus 로고
    • Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution
    • Knapp S, de Vos WM, Rice D, et al. Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3. 0 Å resolution. J Mol Biol, 1997, 267: 916-932.
    • (1997) J Mol Biol , vol.267 , pp. 916-932
    • Knapp, S.1    de Vos, W.M.2    Rice, D.3
  • 5
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: A "traffic rule" for hot roads
    • Karshikoff A, Ladenstein R. Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends Biochem Sci, 2001, 26: 550-556.
    • (2001) Trends Biochem Sci , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 6
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution
    • Russell R J, Ferguson J M, Hough D W, et al. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1. 9 Å resolution. Biochemistry, 1997, 36: 9983-9994.
    • (1997) Biochemistry , vol.36 , pp. 9983-9994
    • Russell, R.J.1    Ferguson, J.M.2    Hough, D.W.3
  • 8
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G, Woell S, Argos P. Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol, 1997, 269: 631-643.
    • (1997) J Mol Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 9
    • 0035050561 scopus 로고    scopus 로고
    • Crystal structure of Bacillus stearothermophilus alpha-amylase: Possible factors determining the thermostability
    • Tokyo
    • Suvd D, Fujimoto Z, Takase K, et al. Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability. J Biochem (Tokyo), 2001, 129: 461-468.
    • (2001) J Biochem , vol.129 , pp. 461-468
    • Suvd, D.1    Fujimoto, Z.2    Takase, K.3
  • 10
    • 0026655355 scopus 로고
    • Increasing the thermostability of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding
    • Eijsink V G, Vriend G, van der Zee J R, et al. Increasing the thermostability of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding. Biochem J, 1992, 285: 625-628.
    • (1992) Biochem J , vol.285 , pp. 625-628
    • Eijsink, V.G.1    Vriend, G.2    van der Zee, J.R.3
  • 11
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 angstroms resolution
    • Tanner J J, Hecht R M, Krause K L. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 angstroms resolution. Biochemistry, 1996, 35: 2597-2609.
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 12
    • 34547748376 scopus 로고    scopus 로고
    • Implication for buried polar contacts and ion pairs in hyperthermostable enzymes
    • Matsui I, Harata K. Implication for buried polar contacts and ion pairs in hyperthermostable enzymes. FEBS J, 2007, 274: 4012-4022.
    • (2007) FEBS J , vol.274 , pp. 4012-4022
    • Matsui, I.1    Harata, K.2
  • 13
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • Bae E, Phillips G N Jr. Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J Biol Chem, 2004, 279: 28202-28208.
    • (2004) J Biol Chem , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips Jr., G.N.2
  • 14
    • 67349172630 scopus 로고    scopus 로고
    • Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus
    • Del Vecchio P, Elias M, Merone L, et al. Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus. Extremophiles, 2009, 13: 461-470.
    • (2009) Extremophiles , vol.13 , pp. 461-470
    • del Vecchio, P.1    Elias, M.2    Merone, L.3
  • 15
    • 38149111171 scopus 로고    scopus 로고
    • Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins
    • Zhou X X, Wang Y B, Pan Y J, et al. Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins. Amino Acids, 2008, 34: 25-33.
    • (2008) Amino Acids , vol.34 , pp. 25-33
    • Zhou, X.X.1    Wang, Y.B.2    Pan, Y.J.3
  • 16
    • 0022913003 scopus 로고
    • Transport of trehalose in Salmonella typhimurium
    • Postma P W, Keizer H G, Koolwijk P. Transport of trehalose in Salmonella typhimurium. J Bacteriol, 1986, 168: 1107-1111.
    • (1986) J Bacteriol , vol.168 , pp. 1107-1111
    • Postma, P.W.1    Keizer, H.G.2    Koolwijk, P.3
  • 17
    • 0036829797 scopus 로고    scopus 로고
    • Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system
    • Cornilescu G, Lee B R, Cornilescu C C, et al. Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system. J Biol Chem, 2002, 277: 42289-42298.
    • (2002) J Biol Chem , vol.277 , pp. 42289-42298
    • Cornilescu, G.1    Lee, B.R.2    Cornilescu, C.C.3
  • 18
    • 0026660314 scopus 로고
    • Site-specific mutagenesis of residues in the Escherichia coli mannitol permease that have been suggested to be important for its phosphorylation and chemoreception functions
    • Weng Q P, Elder J, Jacobson G R. Site-specific mutagenesis of residues in the Escherichia coli mannitol permease that have been suggested to be important for its phosphorylation and chemoreception functions. J Biol Chem, 1992, 267: 19529-19535.
    • (1992) J Biol Chem , vol.267 , pp. 19529-19535
    • Weng, Q.P.1    Elder, J.2    Jacobson, G.R.3
  • 19
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma P W, Lengeler J W, Jacobson G R. Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria. Microbiol Rev, 1993, 57: 543-594.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 20
    • 14844316751 scopus 로고    scopus 로고
    • HPr as a model protein in structure, interaction, folding and stability studies
    • Azuaga A I, Neira J L, van Nuland N A. HPr as a model protein in structure, interaction, folding and stability studies. Protein Pept Lett, 2005, 12: 123-137.
    • (2005) Protein Pept Lett , vol.12 , pp. 123-137
    • Azuaga, A.I.1    Neira, J.L.2    van Nuland, N.A.3
  • 21
    • 0027340388 scopus 로고
    • The 2.0-Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination
    • Jia Z, Quail J W, Waygood E B, et al. The 2. 0-Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination. J Biol Chem, 1993, 268: 22490-22501.
    • (1993) J Biol Chem , vol.268 , pp. 22490-22501
    • Jia, Z.1    Quail, J.W.2    Waygood, E.B.3
  • 22
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis 2.0-Å resolution
    • Herzberg O, Reddy P, Sutrina S, et al. Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis 2. 0-Å resolution. Proc Natl Acad Sci USA, 1992, 89: 2499-2503.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2499-2503
    • Herzberg, O.1    Reddy, P.2    Sutrina, S.3
  • 23
    • 0028056155 scopus 로고
    • The 1.6 Å structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis
    • Jia Z, Vandonselaar M, Hengstenberg W, et al. The 1. 6 Å structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis. J Mol Biol, 1994, 236: 1341-1355.
    • (1994) J Mol Biol , vol.236 , pp. 1341-1355
    • Jia, Z.1    Vandonselaar, M.2    Hengstenberg, W.3
  • 24
    • 0029645286 scopus 로고
    • Structural evidence for the evolutionary divergence of Mycoplasma from gram-positive bacteria-the histidine-containing phosphocarrier protein
    • Pieper U, Kapadia G, Zhu P P, et al. Structural evidence for the evolutionary divergence of Mycoplasma from gram-positive bacteria-the histidine-containing phosphocarrier protein. Structure, 1995, 3: 781-790.
    • (1995) Structure , vol.3 , pp. 781-790
    • Pieper, U.1    Kapadia, G.2    Zhu, P.P.3
  • 25
    • 0027098199 scopus 로고
    • Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy
    • Wittekind M, Rajagopal P, Branchini B R, et al. Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy. Protein Sci, 1992, 1: 1363-1376.
    • (1992) Protein Sci , vol.1 , pp. 1363-1376
    • Wittekind, M.1    Rajagopal, P.2    Branchini, B.R.3
  • 26
    • 0022925241 scopus 로고
    • Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR
    • Klevit R E, Waygood E B. Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR. Biochemistry, 1986, 25: 7774-7781.
    • (1986) Biochemistry , vol.25 , pp. 7774-7781
    • Klevit, R.E.1    Waygood, E.B.2
  • 27
    • 79959603624 scopus 로고    scopus 로고
    • Expression, crystallization and characterization of a novel 6-phospho-β-glucosidase from Thermoanaerobacter tengcongensis MB4
    • Yin J, Liu Y, Li J, et al. Expression, crystallization and characterization of a novel 6-phospho-β-glucosidase from Thermoanaerobacter tengcongensis MB4. Chin J Biochem Mol Biol, 2008, 24: 916-924.
    • (2008) Chin J Biochem Mol Biol , vol.24 , pp. 916-924
    • Yin, J.1    Liu, Y.2    Li, J.3
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, Carter C W, et al. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol, 1997, 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Carter, C.W.3
  • 29
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Crystallogr, 1997, 30: 1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G N, Vagin A A, Dodson E J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D, 1997, 53: 240-255.
    • (1997) Acta Cryst D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Cryst D, 2004, 60: 2126-2132.
    • (2004) Acta Cryst D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 32
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams P D, Grosse-Kunstleve R W, Hung L W, et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr, 2002, 58: 1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1    Grosse-Kunstleve, R.W.2    Hung, L.W.3
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R A, MacArthur M W, Moss D S, et al. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr, 1993, 26: 283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3
  • 34
    • 0021112481 scopus 로고
    • Ion-pairs in proteins
    • Barlow D, Thornton J. Ion-pairs in proteins. J Mol Biol, 1983, 168: 867-885.
    • (1983) J Mol Biol , vol.168 , pp. 867-885
    • Barlow, D.1    Thornton, J.2
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Cryst D, 1994, 50: 760-763.
    • (1994) Acta Cryst D , vol.50 , pp. 760-763
  • 36
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph, 1990, 8: 52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 38
    • 33645554971 scopus 로고    scopus 로고
    • A thermodynamic comparison of HPr proteins from extremophilic organisms
    • Razvi A, Scholtz J M. A thermodynamic comparison of HPr proteins from extremophilic organisms. Biochemistry, 2006, 45: 4084-4092.
    • (2006) Biochemistry , vol.45 , pp. 4084-4092
    • Razvi, A.1    Scholtz, J.M.2
  • 40
    • 35648949313 scopus 로고    scopus 로고
    • Effects of histidine protonation and phosphorylation on histidine-containing phosphocarrier protein structure, dynamics, and physicochemical properties
    • Homeyer N, Essigke T, Ullmann G M, et al. Effects of histidine protonation and phosphorylation on histidine-containing phosphocarrier protein structure, dynamics, and physicochemical properties. Biochemistry, 2007, 46: 12314-12326.
    • (2007) Biochemistry , vol.46 , pp. 12314-12326
    • Homeyer, N.1    Essigke, T.2    Ullmann, G.M.3
  • 41
    • 17644365489 scopus 로고    scopus 로고
    • Structural features of thermozymes
    • Li W F, Zhou X X, Lu P. Structural features of thermozymes. Biotechnol Adv, 2005, 23: 271-281.
    • (2005) Biotechnol Adv , vol.23 , pp. 271-281
    • Li, W.F.1    Zhou, X.X.2    Lu, P.3
  • 42
    • 78650695290 scopus 로고    scopus 로고
    • Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions
    • Ben M S, Aghajari N, Ben A M, et al. Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions. Bioresour Technol, 2011, 102: 1740-1746.
    • (2011) Bioresour Technol , vol.102 , pp. 1740-1746
    • Ben, M.S.1    Aghajari, N.2    Ben, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.