메뉴 건너뛰기




Volumn 57, Issue 2, 2004, Pages 422-431

X-ray structure of a membrane-bound β-glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii

Author keywords

Alkylglucosides; Docking simulation; Glycosyl hydrolase; Hyperthermophile; Membrane bound enzyme; Thermostability

Indexed keywords

ENZYME; GLYCOLIPID; GLYCOSIDASE; GLYCOSIDE; MEMBRANE ENZYME; OLIGOSACCHARIDE; PHOSPHATE; SURFACTANT;

EID: 4544387644     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20203     Document Type: Article
Times cited : (26)

References (42)
  • 1
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 1991;280:309-316.
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 1993;293:781-788.
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 3
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymatic glycosyl transfer
    • Sinnott ML. Catalytic mechanisms of enzymatic glycosyl transfer. ChemRev 1990;90:1171-1202.
    • (1990) ChemRev , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 4
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G, Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995;3:853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 5
    • 0028956984 scopus 로고
    • β-Glucosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxyterminal ends of β-strands four and seven
    • Jenkins J, Lo Leggio L, Harris G, Pickersgill R. β-Glucosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxyterminal ends of β-strands four and seven. FEBS Lett 1995;362: 281-285.
    • (1995) FEBS Lett , vol.362 , pp. 281-285
    • Jenkins, J.1    Lo Leggio, L.2    Harris, G.3    Pickersgill, R.4
  • 6
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA 1995;92:7090-7094.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 7
    • 0029645415 scopus 로고
    • The three-dimensional structure of 6-phospho-β-galactosidase from Lactococcus lactis
    • Wiesmann C, Beste G, Hengstenberg W, Schulz GE. The three-dimensional structure of 6-phospho-β-galactosidase from Lactococcus lactis. Structure 1995;3:961-968.
    • (1995) Structure , vol.3 , pp. 961-968
    • Wiesmann, C.1    Beste, G.2    Hengstenberg, W.3    Schulz, G.E.4
  • 8
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T, Suresh CG, Tolley SP, Dodson EJ, Hughes MA. The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 1995;3:951-960.
    • (1995) Structure , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 9
    • 0031570331 scopus 로고    scopus 로고
    • The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an s-glycosidase
    • Burmeister WP, Cottaz S, Driguez H, Iori R, Palmieri S, Henrissat B. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an s-glycosidase. Structure 1997;5:663-675.
    • (1997) Structure , vol.5 , pp. 663-675
    • Burmeister, W.P.1    Cottaz, S.2    Driguez, H.3    Iori, R.4    Palmieri, S.5    Henrissat, B.6
  • 10
    • 0032559380 scopus 로고    scopus 로고
    • Crystal structure of β-glucosidase A from Bacillus polymyxa: Insights into the catalytic activity in family 1 glycosyl hydrolases
    • Sanz-Aparicio J, Hermoso JA, Martinez-Ripoll M, Lequerica JL, Polaina J. Crystal structure of β-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases. J Mol Biol 1998;275:491-502.
    • (1998) J Mol Biol , vol.275 , pp. 491-502
    • Sanz-Aparicio, J.1    Hermoso, J.A.2    Martinez-Ripoll, M.3    Lequerica, J.L.4    Polaina, J.5
  • 11
    • 0031554925 scopus 로고    scopus 로고
    • Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: Resilience as a key factor in thermostability
    • Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, Pearl LH. Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J Mol Biol 1997;271:789-802.
    • (1997) J Mol Biol , vol.271 , pp. 789-802
    • Aguilar, C.F.1    Sanderson, I.2    Moracci, M.3    Ciaramella, M.4    Nucci, R.5    Rossi, M.6    Pearl, L.H.7
  • 12
    • 0032982023 scopus 로고    scopus 로고
    • Crystal structure of the β-glycosidase from the hyperthermophile Thermosphaera aggregans: Insights into its activity and thermostability
    • Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH. Crystal structure of the β-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability. FEBS Lett 1999;445:375-383.
    • (1999) FEBS Lett , vol.445 , pp. 375-383
    • Chi, Y.I.1    Martinez-Cruz, L.A.2    Jancarik, J.3    Swanson, R.V.4    Robertson, D.E.5    Kim, S.H.6
  • 13
    • 0033977063 scopus 로고    scopus 로고
    • Novel substrate specificity of a membrane-bound β-glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii
    • Matsui I, Sakai Y, Matsui E, Kikuchi H, Kawarabayasi Y, Honda K. Novel substrate specificity of a membrane-bound β-glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii. FEBS Lett 2000;467:195-200.
    • (2000) FEBS Lett , vol.467 , pp. 195-200
    • Matsui, I.1    Sakai, Y.2    Matsui, E.3    Kikuchi, H.4    Kawarabayasi, Y.5    Honda, K.6
  • 15
    • 0002033068 scopus 로고    scopus 로고
    • MOSFLM - Recent changes and future developments
    • Leslie AGW. MOSFLM- recent changes and future developments. CCP4 Newslett Protein Crystallogr 1998;35:18-19.
    • (1998) CCP4 Newslett Protein Crystallogr , vol.35 , pp. 18-19
    • Leslie, A.G.W.1
  • 16
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 18
    • 0002771888 scopus 로고
    • TURBO-FRODO: A tool for building structural models
    • Silicon Graphics, editor. Mountain View: Silicon Graphics
    • Roussel A, Cambillau C. TURBO-FRODO: a tool for building structural models. In: Silicon Graphics, editor. Silicon Graphics Geometry Partners Directory. Mountain View: Silicon Graphics; 1991. p 86.
    • (1991) Silicon Graphics Geometry Partners Directory , pp. 86
    • Roussel, A.1    Cambillau, C.2
  • 19
  • 20
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. Molscript - a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24: 946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0028057108 scopus 로고
    • Raster3d Version-2.0 - A program for photorealistic molecular graphics
    • Merritt EA, Murphy MEP. Raster3d Version-2.0 - a program for photorealistic molecular graphics. Acta Crystallogr D Biol Crystallogr 1994;50:869-873.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 23
    • 0023656847 scopus 로고
    • The crystal structures of octyl α-D-glucopyranoside monohydrate and hemihydrate: Mesogenic structures with interdigitizing alkyl chains
    • Jeffrey GA, Yeon Y, Abola J. The crystal structures of octyl α-D-glucopyranoside monohydrate and hemihydrate: mesogenic structures with interdigitizing alkyl chains. Carbohydr Res 1987; 169:1-11.
    • (1987) Carbohydr Res , vol.169 , pp. 1-11
    • Jeffrey, G.A.1    Yeon, Y.2    Abola, J.3
  • 25
    • 0041705990 scopus 로고    scopus 로고
    • Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton
    • Chang SY, Ko TP, Liang PH, Wang AH. Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton. J Biol Chem 2003;278:29298-29307.
    • (2003) J Biol Chem , vol.278 , pp. 29298-29307
    • Chang, S.Y.1    Ko, T.P.2    Liang, P.H.3    Wang, A.H.4
  • 26
    • 0022578265 scopus 로고
    • Structure, biosynthesis, and physicochemical properties of archaebacterial lipids
    • De Rosa M, Gambacorta A, Gliozzi A. Structure, biosynthesis, and physicochemical properties of archaebacterial lipids. Microbiol Rev 1986;50:70-80.
    • (1986) Microbiol Rev , vol.50 , pp. 70-80
    • De Rosa, M.1    Gambacorta, A.2    Gliozzi, A.3
  • 27
    • 0027401021 scopus 로고
    • Ether polar lipids of methanogenic bacteria: Structures, comparative aspects, and biosyntheses
    • Koga Y, Nishihara M, Morii H, Akagawa-Matsushita M. Ether polar lipids of methanogenic bacteria: structures, comparative aspects, and biosyntheses. Microbiol Rev 1993;57:164-182.
    • (1993) Microbiol Rev , vol.57 , pp. 164-182
    • Koga, Y.1    Nishihara, M.2    Morii, H.3    Akagawa-Matsushita, M.4
  • 28
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke R, Schurig H, Beaucamp N, Ostendorp R. Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Adv Protein Chem 1996;48:181-269.
    • (1996) Adv Protein Chem , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 29
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch ZS, Tidor. B. Do salt bridges stabilize proteins?: a continuum electrostatic analysis. Protein Sci 1994;3:211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 30
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer I, Steipe B, Huber R, Tomschy A, Jaenicke R. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J Mol Biol 1995;246:511-521.
    • (1995) J Mol Biol , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 31
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability
    • Lim J-H, Yu YG, Han YS, Cho S-j, Ahn B-Y, Kim S-H, Cho Y. The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: structural basis for thermostability. J Mol Biol 1997;270:259-274.
    • (1997) J Mol Biol , vol.270 , pp. 259-274
    • Lim, J.-H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.-J.4    Ahn, B.-Y.5    Kim, S.-H.6    Cho, Y.7
  • 32
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • Elcock AH. The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J Mol Biol 1998;284: 489-502.
    • (1998) J Mol Biol , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 33
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • Cambillau C, Claverie JM. Structural and genomic correlates of hyperthermostability. J Biol Chem 2000;275:32383-32386.
    • (2000) J Biol Chem , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.M.2
  • 34
    • 0035876479 scopus 로고    scopus 로고
    • Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria
    • Fukuchi S, Nishikawa K. Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria. J Mol Biol 2001;309:835-843.
    • (2001) J Mol Biol , vol.309 , pp. 835-843
    • Fukuchi, S.1    Nishikawa, K.2
  • 35
    • 0028001306 scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of a type I β-glucosidase encoded by the bgIA gene of Bacillus polymyxa
    • Sanz-Aparicio J, Romero A, Martinez-Ripoll M, Madarro A, Flors A,. Polaina J. Crystallization and preliminary X-ray diffraction analysis of a type I β-glucosidase encoded by the bgIA gene of Bacillus polymyxa. J Mol Biol 1994;240:267-270.
    • (1994) J Mol Biol , vol.240 , pp. 267-270
    • Sanz-Aparicio, J.1    Romero, A.2    Martinez-Ripoll, M.3    Madarro, A.4    Flors, A.5    Polaina, J.6
  • 37
    • 0036643503 scopus 로고    scopus 로고
    • Ionic network at the C-terminus of the β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization
    • Cobucci-Ponzano B, Moracci M, Di Lauro B, Ciaramella M, D'Avino R, Rossi M. Ionic network at the C-terminus of the β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: functional role in the quaternary structure thermal stabilization. Proteins 2002;48:98-106.
    • (2002) Proteins , vol.48 , pp. 98-106
    • Cobucci-Ponzano, B.1    Moracci, M.2    Di Lauro, B.3    Ciaramella, M.4    D'Avino, R.5    Rossi, M.6
  • 39
    • 0032934819 scopus 로고    scopus 로고
    • A revised model of the active site of alternative oxidase
    • Andersson ME, Nordlund P. A revised model of the active site of alternative oxidase. FEBS Lett 1999;449:17-22.
    • (1999) FEBS Lett , vol.449 , pp. 17-22
    • Andersson, M.E.1    Nordlund, P.2
  • 40
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian JA, von Heijne G. How proteins adapt to a membrane-water interface. Trends Biochem Sci 2000;25:429-434.
    • (2000) Trends Biochem Sci , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 42
    • 84986486656 scopus 로고
    • A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls A, Honig B. A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J Comput Chem 1991;12:435-445.
    • (1991) J Comput Chem , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.