Crystal structure of a pH-stabilized mutant of villin headpiece

Biochemistry

Volumn 47, Issue 16, 2008, Pages 4644-4650

  Meng, Jianmin ^a,b   McKnight, C James ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CRYSTAL STRUCTURE; HYDROPHOBICITY; PH EFFECTS; SENSITIVITY ANALYSIS; SUBSTITUTION REACTIONS;

HYDROXYL GROUPS; TERMINAL SUBDOMAINS;

PROTEIN FOLDING;

CARBONYL DERIVATIVE; F ACTIN; HISTIDINE; HYDROXYL GROUP; IMIDAZOLE DERIVATIVE; MUTANT PROTEIN; TYROSINE; VILLIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; HYDROGEN BOND; HYDROPHOBICITY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTON TRANSPORT; THERMOSTABILITY;

ACTINS; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; MODELS, MOLECULAR; MUTATION; NEUROFILAMENT PROTEINS; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 42349095733     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7022738     Document Type: Article

References (27)

1. Glenney, J. R., Jr., Geisler, N., Kaulfus, P., and Weber, K. (1981) Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization. J. Biol. Chem. 256, 8156-8161.
2. Vardar, D., Chishti, A. H., Frank, B. S., Luna, E. J., Noegel, A. A., Oh, S. W., and McKnight, C. J. (2002) Villin-type headpiece domains show a wide range of F-actin-binding affinities. Cell Motil. Cytoskeleton 52, 9-21.
3. Meng, J., Vardar, D., Wang, Y., Guo, H., Head, J., and McKnight, C. (2005) High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity. Biochemistry 44, 11963-11973.
4. Vardar, D., Buckley, D., Frank, B., and McKnight, C. (1999) NMR structure of an F-actin binding "headpiece" motif from villin. J. Mol. Biol. 249, 1299-1310.
5. Kubelka, J., Eaton, W. A., and Hofrichter, J. (2003) Experimental tests of villin subdomain folding simulations. J. Mol. Biol. 329, 625-630.
6. McKnight, C. J., Doering, D. S., Matsudaira, P. T., and Kim, P. S. (1996) A thermostable 35-residue subdomain within villin headpiece. J. Mol. Biol. 260, 126-134.
7. Wang, M., Tang, Y., Sato, S., Vugmeyster, L., McKnight, C. J., and Raleigh, D. P. (2003) Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. J. Am. Chem. Soc. 125, 6032-6033.
8. Doering, D. S., and Matsudaira, P. T. (1996) Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 35, 12677-12685.
9. Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J., and Louvard, D. (1992) An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70, 81-92.
10. Vermeulen, W., Vanhaesebrouck, P., Van Troys, M., Verschueren, M., Fant, F., Goethals, M., Ampe, C., Martins, J. C., and Borremans, F. A. (2004) Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements. Protein Sci. 13, 1276-1287.
11. Chiu, T. K., Kubelka, J., Herbst-Irmer, R., Eaton, W. A., Hofrichter, J., and Davies, D. R. (2005) High-resolution X-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein. Proc. Natl. Acad. Sci. U.S.A. 102, 7517-7522.
12. McKnight, C. J., Matsudaira, P. T., and Kim, P. S. (1997) NMR structure of the 35-residue villin headpiece subdomain. Nat. Struct. Biol. 4, 180-184.
13. Vugmeyster, L., Trott, O., McKnight, C. J., Raleigh, D. P., and Palmer, A. G., III (2002) Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein. J. Mol. Biol. 320, 841-854.
14. Yang, A. S., and Honig, B. (1993) On the pH dependence of protein stability. J. Mol. Biol. 231, 459-474.
15. Tang, Y., Grey, M. J., McKnight, J., Palmer, A. G., III, and Raleigh, D. P. (2006) Multistate folding of the villin headpiece domain. J. Mol. Biol. 355, 1066-1077.
16. Grey, M. J., Tang, Y., Alexov, E., McKnight, C. J., Raleigh, D. P., and Palmer, A. G., III (2006) Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: Contribution of His41 to the pH-dependent stability of the N-terminal subdomain. J. Mol. Biol. 355, 1078-1094.
17. Pardee, J. D., and Spudich, J. A. (1982) Purification of muscle actin. Methods Enzymol. 85, 164-181.
18. Edelhoch, H. (1948) (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1954.
19. Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988) Improved staining of proteins in Polyacrylamide gels including isoelectric-focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 255-262.
20. Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
21. Jones, T. A., Zou, J. Y., and Cowan, S. W. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., Sect. A: Found. Crystallogr. 47 (part 2), 110-119.
22. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr, Sect. D: Biol. Crystallogr. 54, 905-921.
23. Chou, P. Y., and Fasman, G. D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 47, 45-148.
24. Chou, P. Y., and Fasman, G. D. (1978) Empirical predictions of protein conformation. Annu. Rev. Biochem. 47, 251-276.
25. Swillens, S. (1995) Interpretation of binding curves obtained with high receptor concentrations - Practical aid for computer analysis. Mol. Pharmacol. 47, 1197-1203.
26. Pelton, J. G., Torchia, D. A., Meadow, N. D., and Roseman, S. (1993) Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci. 2, 543-558.
27. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures. J Mol. Graphics 14, 51-55.