Elucidation of information encoded in tryptophan 140 of staphylococcal nuclease

Proteins: Structure, Function and Genetics

Volumn 58, Issue 2, 2005, Pages 271-277

  Hirano, Satoshi ^a,b   Kamikubo, Hironari ^a   Yamazaki, Yoichi ^a   Kataoka, Mikio ^a  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b INSTITUTE OF MATERIALS STRUCTURE SCIENCE   (Japan)

Author keywords

Circular dichroism; Hydrolysis of DNA; Protein folding; Sequence structure relationship; Structure function relationship; Substitution mutant; X ray solution scattering

Indexed keywords

INDOLE; MUTANT PROTEIN; NITROGEN; NUCLEASE; TRYPTOPHAN DERIVATIVE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SUBSTRATE; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; STAPHYLOCOCCUS; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY;

CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; MAGNETIC RESONANCE SPECTROSCOPY; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; MUTATION; NITROGEN; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEOMICS; SCATTERING, RADIATION; THERMODYNAMICS; TRYPTOPHAN; X-RAYS;

EID: 11344258621     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20333     Document Type: Article

References (30)

1. Dobson CM. Protein folding and misfolding. Nature 2003;426:884-890.
2. Onuchic JN, Socci ND, Luthey-Shulten Z, Wolynes PG. Protein folding funnels: the nature of the transition state ensemble. Fold Des 1996;1:441-450.
3. Dill KA, Chan HS. From Levinthal to pathways to funnels. Nat Struct Biol 1997;4:10-19.
4. Baker D. A surprising simplicity to protein folding. Nature 2000;405:39-42.
5. Anfinsen CB. The formation and stabilization of protein structure. Biochem J 1972;128:737-749.
6. Shortle D, Meeker AK, Freire E. Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction. Biochemistry 1988;27:4761-4768.
7. Shortle D, Meeker AK. Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions. Biochemistry 1989;28:936-944.
8. Flanagan JM, Kataoka M, Shortle D, Engelman DM. Truncated staphylococcal nuclease is compact but disordered. Proc Natl Acad Sci USA 1992;89:748-752.
9. Flanagan JM, Kataoka M, Fujisawa T, Engelman DM. Mutations can cause large changes in the conformation of a denatured protein. Biochemistry 1993;32:10359-10370.
10. Jacobs MD, Fox RO. Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy. Proc Natl Acad Sci USA 1994;91:449-453.
11. Kalnin NN, Kuwajima K. Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism. Proteins 1995;23:163-176.
12. Walkenhorst WF, Green SM, Roder H. Kinetic evidence for folding and unfolding intermediates in Staphylococcal nuclease. Biochemistry 1997;36:5795-5805.
13. Walkenhorst WF, Edwards JA, Markley JL, Roder H. Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange. Protein Sci 2002;11:82-91.
14. Kamagata K, Sawano Y, Tanokura M, Kuwajima K. Multiple parallel-pathway folding of proline-free staphylococcal nuclease. J Mol Biol 2003;332:1143-1153.
15. Griko YV, Gittis A, Lattman EE, Privalov PL. Residual structure in a staphylococcal nuclease fragment. Is it a molten globule and is its unfolding a first-order phase transition? J Mol Biol 1994;243:93-99.
16. Kataoka M, Kuwajima K, Tokunaga F, Goto Y. Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering. Protein Sci 1997;6:422-430.
17. Yin J, Jing G. Tryptophan 140 is important, but serine 141 is essential for the formation of the integrated conformation of staphylococcal nuclease. J Biochem 2000;128:113-119.
18. Hirano S, Mihara K, Yamazaki Y, Kamikubo H, Imamoto Y, Kataoka M. Role of C-terminal region of Staphylococcal nuclease for foldability, stability and activity. Proteins 2002;49:255-265.
19. 2+, and the inhibitor pdTp, refined at 1.65 Å. Proteins 1989;5:183-201.
20. Ueki T, Hiragi Y, Kataoka M, Inoko Y, Amemiya Y, Izumi Y, Tagawa H, Muroga Y. Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation. Biophys Chem 1985;23:115-124.
21. Kataoka M, Goto Y. X-ray solution scattering studies of protein folding. Fold Des 1996;1:107-114.
22. Kataoka M, Hagihara Y, Mihara K, Goto Y. Molten globule of cytochrome c studied by small angle X-ray scattering. J Mol Biol 1993;229:591-596.
23. Cuatrecasas P, Fuchs S, Anfinsen CB. Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus. J Biol Chem 1967;242:1541-1547.
24. Shortle D, Abeygunawardana C. NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Structure 1993;1:121-134.
25. Wong CY, Eftink MR. Biosynthetic incorporation of tryptophan analogues into staphylococcal nuclease: effect of 5-hydroxytiyptophan and 7-azatryptophan on structure and stability. Protein Sci 1997;6:689-697.
26. Wong CY, Eftink MR. Incorporation of tryptophan analogues into staphylococcal nuclease, its V66W mutant, and Δ137-149 fragment: spectroscopic studies. Biochemistry 1998;37:8938-8946.
27. Wong CY, Eftink MR. Incorporation of tryptophan analogues into staphylococcal nuclease: stability toward thermal and guanidine-HCl induced unfolding. Biochemistry 1998;37:8947-8953.
28. Yutani K, Takano K, Funahashi J. Evaluation of some factors that contribute to conformational stability of a protein using database of stability/structure. In: Kuwajima K, Arai M, editors. Old and new views of protein folding. Amsterdam: Elsevier Science; 1999. p 205-214.
29. Meeker AK, Garcia-Moreno B, Shortle D. Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. Biochemistry 1996;35:6443-6449.
30. Lamy A, Smith JC. Denaturation of truncated staphylococcal nuclease in molecular dynamics simulation at 300K. J Am Chem Soc 1996;118:7326-7328.