Temperature-dependent structural and functional features of a hyperthermostable enzyme using elastic neutron scattering

Proteins: Structure, Function and Genetics

Volumn 61, Issue 2, 2005, Pages 377-384

  Koutsopoulos, Sotirios ^a,c   Van Der Oost, John ^a   Norde, Willem ^a,b  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c Massachusetts Institute of Technology Cambridge   (United States)

Author keywords

Enzymatic activity; Hyperthermostable enzyme; Neutron scattering; Protein dynamics

Indexed keywords

BACTERIAL ENZYME; RECOMBINANT ENZYME;

ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; NEUTRON SCATTERING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PYROCOCCUS FURIOSUS; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

CALORIMETRY; ENZYME STABILITY; GLUCAN ENDO-1,3-BETA-D-GLUCOSIDASE; MOTION; NEUTRONS; PROTEIN CONFORMATION; PYROCOCCUS FURIOSUS; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE; TEMPERATURE;

PYROCOCCUS FURIOSUS;

EID: 26444594327     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20606     Document Type: Article

References (36)

1. Rothschild LJ, Mancinelli RL. Life in extreme environments. Nature 2001;409:1092-1101.
2. Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 1995;267:1463-1469.
3. Anderson DE, Hurley JH, Nicholson H, Baase WA, Matthews BW. Hydrophobic core repacking and aromatic aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117→Phe. Protein Sci 1993;2:1285-1290.
4. Britton KL, Baker PJ, Borges KM, Engel PC, Pasquo A, Rice DW, Robb FT, Scandurra R, Stillman TJ, Yip KSP. Insights into thermal stability from a comparison of the glutamate-dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis. Eur J Biochem 1995;229:688-695.
5. Russell RJM, Hough DW, Danson MJ, Taylor GL. The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum. Structure 1994;2:1157-1167.
6. Spassov VZ, Karshikoff AD, Ladenstein R. The optimization of protein-solvent interactions-thermostability and the role of hydrophobic and electrostatic interactions. Protein Sci 1995;4:1516-1527.
7. Schumann J, Bohm G, Schumacher G, Rudolph R, Jaenicke R. Stabilization of creatinase from Pseudomonas putida by random mutagenesis. Protein Sci 1993;10:1612-1620.
8. Tanner JJ, Hecht RM, Krause KL. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3- phosphate dehydrogenase at 2.5 angstrom resolution. Biochemistry 1996;35:2597-2609.
9. Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, Pearl LH. Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J Mol Biol 1997;271:789-802.
10. Perutz MF, Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2. Nature 1975;255:256-259.
11. 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-angstrom resolution. J Mol Biol 1995;246:511-521.
12. Russell RJM, Ferguson JMC, Hough DW, Danson MJ, Taylor GL. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 angstrom resolution. Biochemistry 1997;36:9983-9994.
13. Korolev S, Nayal M, Barnes WM, Di Cera E, Waksman G. Crystal structure of the large fragment of Thermus aquaticus DNA-polymerase-i at 2.5-Å resolution - structural basis for thermostability. Proc Natl Acad Sci USA 1995;92:9264-9268.
14. Gueguen Y, Voorhorst WGB, van der Oost J, de Vos WM. Molecular and biochemical characterization of an endo-b-1,3-glucanase of the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 1997;272:31258-31264.
15. Frauenfelder H, Petsko GA, Tsernoglou D. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics. Nature 1979;280:558-563.
16. Karplus M, Petsko GA. Molecular dynamics simulations in biology. Nature 1990;347:631-639.
17. Gerstein M, Lesk AM, Chothia C. Structural mechanisms for domain movements in proteins. Biochemistry 1994;33:6739-6749.
18. Réat V, Dunn R, Ferrand M, Finney JL, Daniel RM, Smith JC. Solvent dependence of dynamic transitions in protein solutions. Proc Natl Acad Sci USA 2000;97:9961-9966.
19. Vitkup D, Ringe D, Petsko GA, Karplus M. Solvent mobility and the protein "glass" transition. Nat Struct Biol 2000;7:34-38.
20. Fenimore PW, Frauenfelder H, McMahon BH, Parak FG. Slaving: solvent fluctuations dominate protein dynamics and functions. Proc Natl Acad Sci USA 2002;99:16047-16051.
21. Zaccai G. How soft is a protein?: a protein dynamics force constant measured by neutron scattering. Science 2000;288:1604-1607.
22. Miller GL. Dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 1959;31:426-428.
23. Smith JC. Protein dynamics: vomparison of simulation with inelastic neutron scattering experiments. Q Rev Biophys 1991;24: 227-291.
24. Ferrand M, Dianoux AJ, Petry W, Zaccai G. Thermal motions and function of bacteriorhodopsin in purple membranes-effects of temperature and hydration studied by neutron-scattering. Proc Natl Acad Sci USA 1993;90:9668-9672.
25. Tehei M, Madern D, Pfister C, Zaccai G. Fast dynamics of halophilic dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability. Proc Natl Acad Sci USA 2001;98:14356-14361.
26. Dunn RE, Réat V, Finney J, Ferrand M, Smith JC, Daniel RM. Enzyme activity and dynamics: xylanase activity in the absence of fast enharmonic dynamics. Biochem J 2000;346:355-358.
27. Daniel RM, Smith JC, Ferrand M, Héry S, Dunn R, Finney JL. Enzyme activity below the dynamical transition at 220 K. Biophys J 1998;75:2504-2507.
28. Bée M. Quasi-elastic neutron scattering: principles and applications in solid state chemistry, biology and materials science. Bristol, UK: Adam Hilger; 1988.
29. Bu Z, Neumann DA, Lee SH, Brown CM, Engelman DM, Han CC. A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering. J Mol Biol 2000;301:525-536.
30. Elber R, Karplus M. Multiple conformational states of proteins - a molecular-dynamics analysis of myoglobin. Science 1987;235:318-321.
31. Noguti T, Go N. Structural basis of hierarchical multiple substates of a protein: II. Monte Carlo simulation of native thermal fluctuations and energy minimization. Proteins 1989;5: 104-112.
32. Frauenfelder H, Sligar GS, Wolynes PG. The energy landscapes and motions of proteins. Science 1991;254:1598-1603.
33. Kim YD, Lumry R. Studies of chymotrypsinogen family of proteins: 13. Inhibitor-induced transient change in fluorescence of alpha-chymotrypsin. J Am Chem Soc 1971;93:1003-1013.
34. Gaily JA, Edelman GM. Effect of temperature on fluorescence of some aromatic amino acids and proteins. Biochim Biophys Acta 1962;60:499-509.
35. Gabel F, Bicout D, Lehnert U, Tehei M, Weik M, Zaccai G. Protein dynamics studied by neutron scattering. Quart Rev Biophys 2002;35:327-367.
36. Liang Z-X, Lee T, Resing KA, Ahn NG, Klinman JP. Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase. Proc Natl Acad Sci USA 2004;101:9556-9561.