Solution structure of switch Arc, a mutant with 310 helices replacing a wild-type β-ribbon

Journal of Molecular Biology

Volumn 326, Issue 3, 2003, Pages 899-909

  Cordes, Matthew H J ^a,c   Walsh, Nathan P ^a   McKnight, C James ^b   Sauer, Robert T ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c University of Arizona   (United States)

Author keywords

Binary pattern; Core packing; NMR structure; Protein evolution; Protein folding

Indexed keywords

PROTEIN; PROTEIN ARC; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; HYDROGEN BOND; METAMORPHOSIS; MOLECULAR INTERACTION; MUTATION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN STRUCTURE; WILD TYPE;

EID: 0037459091     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01425-0     Document Type: Article

References (28)

1. Cordes M.H.J., Walsh N.P., McKnight C.J., Sauer R.T. Evolution of a protein fold in vitro. Science. 284:1999;325-327.
2. Cordes M.H.J., Burton R.E., Walsh N.P., McKnight C.J., Sauer R.T. An evolutionary bridge to a new protein fold. Nature Struct. Biol. 7:2000;1129-1132.
3. Cordes M.H.J., Sauer R.T. Tolerance of a protein to multiple polar-to-hydrophobic surface substitutions. Protein Sci. 8:1999;318-325.
4. 1H NMR spectroscopy. Biochemistry. 28:1989;9826-9833.
5. 13C labeling. Biochemistry. 28:1989;7510-7516.
6. Cai M., Huang Y., Liu J., Krishnamoorthi R. Solution conformations of proline rings in proteins studied by NMR spectroscopy. J. Biomol. NMR. 6:1995;123-128.
7. 1H NMR. Proteins: Struct. Funct. Genet. 17:1993;297-309.
8. Bonvin A.M.J.J., Vis H., Breg J.N., Burgering M.J.M., Boelens R., Kaptein R. Nuclear magnetic resonance solution structure of the Arc repressor using relaxation matrix calculations. J. Mol. Biol. 236:1994;328-341.
9. Nooren I.M.A., Rietveld A.W.M., Melacini G., Sauer R.T., Kaptein R., Boelens R. The solution structure and dynamics of an Arc repressor mutant reveal premelting conformational changes related to DNA binding. Biochemistry. 38:1999;6035-6042.
10. Copley R.R., Barton G.J. A structural analysis of phosphate and sulphate binding sites in proteins. J. Mol. Biol. 242:1994;321-329.
11. Barlow D.J., Thornton J.M. Helix geometry in proteins. J. Mol. Biol. 201:1988;601-619.
12. Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
13. Fleming P.J., Richards F.M. Protein packing: dependence of protein size, secondary structure and amino acid composition. J. Mol. Biol. 299:2000;487-498.
14. Burgering M.J.M., Hald M., Boelens R., Breg J.N., Kaptein R. Hydrogen exchange studies of the Arc repressor: evidence for a monomeric folding intermediate. Biopolymers. 35:1995;217-226.
15. Milla M.E., Sauer R.T. Critical side-chain interactions at a subunit interface in the Arc repressor dimer. Biochemistry. 34:1995;3344-3351.
16. Myers J.K., Pace C.N., Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
17. Miller S., Janin J., Lesk A.M., Chothia C. Interior and surface of monomeric proteins. J. Mol. Biol. 196:1987;641-656.
18. Wang A., Bolen D.W. A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry. 36:1997;9101-9108.
19. Milla M.E., Brown B.M., Sauer R.T. P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences. Protein Sci. 2:1993;2198-2205.
20. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. NMRPipe: a multidmensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:1995;277.
21. Johnson B., Blevins R. NMRView. A computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;603-614.
22. 15N-enriched proteins. J. Am. Chem. Soc. 115:1993;7772-7777.
23. 15N with side chain Hβ resonances in larger proteins. J. Magn. Reson. 95:1991;636-641.
24. Bax A., Vuister G.W., Grzesiek S., Delaglio F., Wang A.C., Tschudin R., Zhu G. Measurement of homo- and heteronuclear J couplings from quantitative J correlation. Methods Enzymol. 239:1994;79-105.
25. Arseniev A., Schultze P., Worgotter E., Braun W., Wagner G., Vask M., et al. Three-dimensional structure of rabbit liver (Cd7) metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J. Mol. Biol. 201:1988;637-657.
26. Brünger A. XPLOR Version 3.1: A System for X-ray Crystallography and NMR. 1993;Yale University Press, New Haven, CT.
27. Laskowski R.A., Rullmann J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;477-486.
28. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.