Abstract
Electrostatic interactions are of considerable importance in protein structure and function, and in a variety of cellular and biochemical processes1–3. Here we report three similar findings from highly refined atomic structures of periplasmic binding proteins. Hydrogen bonds, acting primarily through backbone peptide units, are mainly responsible for the involvement of the positively charged arginine 151 residue in the ligand site of the arabinose-binding protein, for the association between the sulphate-binding protein and the completely buried sulphate dianion, and for the formation of the complex of the leucine/isoleucine/valine-binding protein with the leucine zwitterion. We propose a general mechanism in which the isolated charges on the various buried, desolvated ionic groups are stabilized by the polarized peptide units. This mechanism also has broad application to processes requiring binding of uncompensated ions and charged ligands and stabilization of enzyme reaction charged intermediates, as well as activation of catalytic residues.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Perutz, M. F. Science 201, 1187–1191 (1978).
Matthews, J. B. A Rev. Biophys. biophys. Chem. 14, 387–417 (1985).
Honing, B. H., Hubbel, W. L., & Flewelling, R. T. A Rev. Biophys. biophys. Chem. 15, 163–193 (1986).
Quiocho, F. A. & Vyas, N. K. Nature 310, 381–386 (1984).
Pflugrath, J. W. & Quiocho, F. A. Nature 314, 257–260 (1985).
Vyas, N. K., Vyas, M. N. & Quiocho, F. A. Nature 327, 635–638 (1987).
Quiocho, F. A. et al. in Crystallography in Molecular Biology NATO Series (eds Moras, D. et al.) 385–394 (Plenum, London, 1987).
Lee, B. K. & Richards, F. M. J. molec. Biol. 55, 379–400 (1971).
Saper, M. A. & Quiocho, F. A. J. biol. Chem. 258, 11057–11062 (1983).
Pauling, L. Nature of the Chemical Bond 2nd edn (Cornell University Press, Ithaca, New York, 1960).
Llinas, M. & Klein, M. J. Am. chem. Soc. 97, 4731–4737 (1975).
Wada, A. Adv. Biophys. 9, 1–63 (1976).
Van Duijnen, P. Th. & Thole, B. T. Biopolymers 21, 1749–1761 (1982).
Hol, W. G. J., van Duijnen, P. T. & Berendsen, H. J. C. Nature 273, 443–446 (1978).
Hol, W. G. J. & Wierenga, R. K. in X-Ray Crystallography and Drug Design (eds Horn, A. S. & de Ranter, C. J.) 151–168 (Clarendon, Oxford, 1984).
Smith, W. W. et al. J. molec. Biol. 117, 196–225 (1980).
Berstein, F. C. et al. J. molec. Biol. 112, 535–542 (1977).
Kraut, J. A. Rev. Biochem. 46, 331–358 (1977).
Robertus, J. D. et al. Biochemistry 11, 4293–4203 (1972).
Wierenga, R. K. Trans. Am. cryslallogr. Ass. 22, 49–62 (1986).
Gilliland, G. L. & Quiocho, F. A. J. molec. Biol. 146, 341–362 (1981).
Parsons, R. G. & Hogg, R. W. J. biol. Chem. 249, 3602–3607 (1974).
Pardee, A. B. J. biol. Chem. 241, 5886–5892 (1966).
Penrose, W. R. et al. J. biol. Chem. 243, 5921–5929 (1968).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Quiocho, F., Sack, J. & Vyas, N. Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units. Nature 329, 561–564 (1987). https://doi.org/10.1038/329561a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/329561a0
This article is cited by
-
Tryptophan-galactosylamine conjugates inhibit and disaggregate amyloid fibrils of Aβ42 and hIAPP peptides while reducing their toxicity
Communications Biology (2020)
-
Atomic basis of the exquisite specificity of phosphate and sulfate transport receptors
Kidney International (1996)
-
Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate
Nature (1994)
-
The semiotics of charge
Nature (1991)
-
Structure and function of channels and channelogs as studied by computational chemistry
The Journal of Membrane Biology (1991)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
