The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions

Protein Science

Volumn 6, Issue 6, 1997, Pages 1325-1332

  O'Brien, R ^a   Wynn, R ^b   Driscoll, P C ^a   Davis, B ^a   Plaxco, K W ^c   Sturtevant, J M ^d   Ladbury, J E ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b DUPONT COMPANY   (United States)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d YALE UNIVERSITY   (United States)

Author keywords

Calorimetry; Cysteine modification; Differential scanning; Kinetics; Protein folding; Thermodynamics; Thioredoxin; Unnatural amino acids

Indexed keywords

THIOREDOXIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; DATA ANALYSIS; DISULFIDE BOND; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN FOLDING; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0030960060     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060621     Document Type: Article

References (38)

1. Bax A, Davis DG. 1985. Simplification of H1 NMR spectra by selective excitation of experimental subspectra. J Mag Reson 65:355-360.
2. Briinger AT. 1992. X-PLOR Manual, Version 3.1. New Haven, Connecticut: Yale University.
3. de Lorimier R, Hellinga HW, Spicer LD. 1996. NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin. Protein Sci 5:2552-2565.
4. Dill KA, Shortle D. 1991. Denatured states of proteins. Annu Rev Biochem 60:795-825.
5. Dyson HJ, Gippert GP, Case DA, Holmgren A, Wright PE. 1990. Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. Biochemistry 29:4129-4136.
6. Dyson HJ, Holmgren A, Wright PE. 1989. Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin-Sequence specific assignments, secondary structure, and global fold. Biochemistry 28:7074-7087.
7. Eriksson AE, Baase WA, Zhang XJ, Heinz DW, Blaber M, Baldwin EP, Matthews BW. 1992. Response of a protein structure to cavity-creating mutations. Science 255:178-183.
8. Evans PA, Topping KD, Woolfson DN, Dobson CM. 1991. Hydrophobic clustering in nonnative states of a protein: Interpretation of chemical shifts in NMR spectra of denatured states of lysozyme. Proteins Struc Funct Genet 9:248-266.
9. Fersht AR. 1995. Mapping the structures of transition-states and intermediates in folding: Delineation pathways at high resolution. Phil Trans R Soc 348:11-15.
10. Hellinga HW, Wynn R, Richards FM. 1992. The Hydrophobic core of E. coli thioredoxin shows a high tolerance to non-conservative single amino-acid substitutions. Biochemistry 31:11203-11209.
11. Holmgren A. 1985. Thioredoxin. Ann Rev Biochem 54:237-271.
12. Holmgren A. 1989. Thioredoxin and glutaredoxin systems. J Biol Chem 264: 13963-13966.
13. Holmgren A, Soderberg B. 1970. Crystallization and preliminary crystallgraphic data for thioredoxin from Escherichia coli. J Mol Biol 54:387-390.
14. Hubbard SJ, Gross KH, Argos P. 1994. Intermolecular cavities in globular proteins. Protein Eng 7:613-626.
15. Katti SK, LeMaster DM, Eklund H. 1990. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol 212:167-181.
16. Kelley RF, Richards FM. 1987. Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding. Biochemistry 26:6765-6774.
17. Kelley RF, Shalongo W, Jagannadham MV, Stellwagen E. 1987. Equilibrium and kinetic measurements of conformational transition of reduced thioredoxin. Biochemistry 26:1406-1411.
18. Kelley RF, Stellwagen E. 1984. Conformational transitions of thioredoxin in guanidine hydrochloride. Biochemistry 23:5095-5202.
19. Kelley RF, Wilson JB, Bryant C, Stellwagen E. 1986. Effects of guanidine-hydrochloride on the refolding kinetics of denatured thioredoxin. Biochemistry 25:728-732.
20. Ladbury JE, Kishore N, Hellinga HW, Wynn R, Sturtevant JM. 1994. Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry. Biochemistry 33:3688-3692.
21. Ladbury JE, Wynn R, Hellinga HW, Sturtevant JM. 1993. Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. Biochemistry 32:7526-7530.
22. Ladbury JE, Wynn R, Thomson JA, Sturtevant JM. 1995. Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. Biochemistry 34:2148-2152.
23. Langsetmo K, Fuchs JA, Woodward C. 1991. The conserved buried aspartic acid residue in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. Biochemistry 30:7603-7609.
24. Laskowski R. 1995. SURFNET: A program for visualizing molecular surfaces, cavities, and intermolecular interactions. J Mol Graph 3:323-330.
25. Laurent TC, Moore EC, Reichard P 1964. Enzymatic syntheses of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from E. coli B. J Biol Chem 259:3436-3444.
26. Manning MC, Woody RW. 1987. Theoretical determination of the CD of proteins containing closely packed antiparallel beta sheets. Biopolymers 26:1731-1752.
27. Mark DF, Richardson CC. 1976. Escherichia coli thioredoxin: A subunit of bacteriophage T7 DNA polymcrase. Proc Natl Acad Sci USA 73:780-784.
28. Matthews BW. 1991. Mutational analysis of protein stability. Curr Opin Struct Biol 1:17-21.
29. Mines GA, Torbjörn P, Lee SC, Winkler JA, Gray HB. 1996 Cytochrome C folding triggered by electron transfer. Chem & Biol 3:491-497.
30. O'Brien RRJ. 1994. The biochemical and biophysical properties of xylanases I and II from Trichoderma viride. [PhD thesis]. London: University of Greenwich.
31. Reutimann H, Straub B, Luisi P-L, Holmgren A. 1981. A conformational study of thioredoxin and its tryptic fragments. J Biol Chem 256:6796-6803.
32. Richards FM. 1977. Areas, volumes packing, and protein structures. Annu Rev Biophys Bioeng 6:151-176.
33. Richards FM, Lim WA. 1994. An analysis of packing in the protein folding problem. Annu Rev Biophys Bioeng 26:423-498.
34. Santoro MM, Bolen DW. 1992. A test of the linear extrapolation of unfolding free energy change over an extended denaturant concentration range. Biochemistry 31:4901-4907.
35. Sturtevant JM. 1987. Biochemical applications of differential scanning calorimetry. Annu Rev Phys Chem 38:463-488.
36. Tanaka A, Flanagan J, Sturtevant JM. 1993. Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studies by differential scanning calorimetry. Protein Sci 2:567-576.
37. Wynn R, Harkins PC, Richards FM, Fox RO. 1996. Mobile unnatural amino acid side chains in the core of staphylococcal nuclease. Protein Sci 5:1026-1031.
38. Wynn R, Richards FM. 1993. Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques. Protein Sci 2:395-403.