Summary
The oxidized form of the mercuric ion binding protein MerP has been studied by two-dimensional NMR. MerP, which is a periplasmic water-soluble protein with 72 amino acids, is involved in the detoxification of mercuric ions in bacteria with resistance against mercury. The mercuric ions in the periplasmic space are first scavenged by the MerP protein, then transported into the cytoplasm by the membrane-bound transport protein MerT, and finally reduced to elementary (nontoxic) mercury by the enzyme mercuric reductase. In this work, the 1H NMR spectrum of oxidized MerP (closed disulfide bridge) has been assigned by using homonuclear 2D NMR techniques. The secondary structure and global fold have been inferred from the nuclear Overhauser effect (NOE) data. The secondary structure comprises four β-strands and two α-helices, in the order β1α1β2β3α2β4. The protein folds into an antiparallel β-sheet, β2β3β1β4, with the two antiparallel helices on one side of the sheet. The folding topology is similar to that of acylphosphatase, the activation domain of porcine pancreatic procarboxypeptidase B, the DNA-binding domain of bovine papillomavirus-1 E2 and the RNA-binding domains of the U1 snRNP A and hnRNP C proteins. However, there is no structural similarity between MerP and other bacterial periplasmic binding proteins.
Similar content being viewed by others
References
Ames G.F.-L., Mimura C.S. and Shyamala V. (1990) FEMS Microbiol. Rev. 75, 429–446.
Aue W.P., Bartholdi E. and Ernst R.R. (1976) J. Chem. Phys., 64, 2229–2246.
Barrineau P., Gilbert P., Jackson W.J., Jones C.S., Summers A.O. and Wisdom S. (1984) J. Mol. Appl. Genet., 2, 601–619.
Bax A. and Davis D.G. (1985) J. Magn. Reson., 65, 355–360.
Bax A. and Drobny G. (1985) J. Magn. Reson., 61, 306–320.
Bodenhausen G., Vold R.L. and Vold R.R. (1980) J. Magn. Reson., 37, 93–106.
Braunschweiler L., Bodenhausen G. and Ernst R.R. (1983) Molec. Phys., 48, 535–560.
Braunschweiler L. and Ernst R.R. (1983) J. Magn. Reson., 53, 521–528.
Brown N.L. (1985) Trends Biochem. Sci., 10, 400–403.
Brown S.C., Weber P.L. and Mueller L. (1988) J. Magn. Reson., 77, 166–169.
Callaghan P.T., MacKay A.L., Pauls K.P., Söderman O. and Bloom M. (1984) J. Magn. Reson., 56, 101–109.
Chazin W.J. and Wright P.E. (1987) Biopolymers, 26, 973–977.
Coll M., Guasch A., Avilés F.X. and Huber R. (1991) EMBO J., 191, 1–9.
Creighton T.E. (1983) Proteins, Structures and Molecular Properties, W.H. Freeman and Company, New York, p. 230.
Drobny G., Pines A., Sinton S., Weitekamp D. and Wemmer D. (1979) Faraday Div. Chem. Soc. Symp., 13, 49–55.
Eich G., Bodenhausen G. and Ernst R.R. (1982) J. Am. Chem. Soc., 104, 3732–3733.
Eisenberg D., Wesson M. and Wilcox W. (1989) In Prediction of Protein Structure and the Principles of Protein Conformation (Ed., Fasman G.D.) Plenum Press, New York, pp. 635–646.
Griesinger C., Otting G., Wüthrich K. and Ernst R.R. (1988) J. Am. Chem. Soc., 110, 7870–7872.
Gross K.H. and Kalbitzer H.R. (1988) J. Magn. Reson., 76, 87–99.
Hamlett N.V., Landale E.C., Davis B.H. and Summers A.O. (1992) J. Bacteriol., 174, 6377–6385.
Hegde R.S., Grossman S.R., Laimins L.A. and Sigler P.B. (1992) Nature, 359, 505–512.
Jeener J., Meier B.H., Backmann P. and Ernst R.R. (1979) J. Chem. Phys., 71, 4546–4553.
Kumar A., Ernst R.R. and Wüthrich K. (1980) Biochem. Biophys. Res. Commun., 95, 1–6.
Leijonmarck M. and Liljas A. (1987) J. Mol. Biol., 195, 555–580.
Manoleras N. and Norton R. (1972) J. Biomol. NMR, 2, 485–494.
Marion D. and Bax A. (1988) J. Magn. Reson., 79, 352–356.
Marion D. and Bax A. (1989) J. Magn. Reson., 83, 205–211.
Marion D., Ikura M. and Bax A. (1989) J. Magn. Reson., 84, 425–430.
Marion D. and Wüthrich K. (1983) Biochem. Biophys. Res. Comm., 113, 967–974.
Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M., Haberstroh L. and Silver S. (1984) Proc. Natl. Acad. Sci. USA, 81, 5975–5979.
Nagai K., Oubridge C., Jessen T.H., Li J. and Evans P.R. (1990) Nature, 348, 515–520.
Pastore A., Saudek V., Ramponni G. and Williams R.J.P. (1992) J. Mol. Biol., 224, 427–440.
Pelczer I. (1991) J. Am. Chem. Soc., 113, 3211–3212.
Quiocho F.A. (1990) Phil. Trans. R. Soc. Lond. B., 326, 341–351.
Quiocho F.A. and Vyas N.K. (1984) Nature, 310, 381–386.
Rance M., Sørensen O.W., Bodenhausen G., Wagner G., Ernst R.R. and Wüthrich K. (1983) Biochem. Biophys. Res. Commun., 117, 479–485.
Rance M., Sørensen O.W., Leupin W., Kogler H., Wüthrich K. and Ernst R.R. (1985) J. Magn. Reson., 61, 67–80.
Richardson J. (1981) Adv. Protein Chem., 34, 167–339.
Sahlman L. and Jonsson B.-H. (1992) Eur. J. Biochem., 205, 375–381.
Summers A.O. (1986) Annu. Rev. Microbiol., 40, 607–634.
Vendrell J., Billeter M., Wider G., Avilés F.X. and Wüthrich K. (1991) EMBO J., 10, 11–15.
Wagner G. (1983) J. Wagn. Reson., 55, 151–156.
Wishart D.S., Sykes B.D. and Richards F.M. (1992) Biochemistry, 31, 1647–1651.
WilliamsJr. C.H. (1992) In Chemistry and Biochemistry of Flavoenzymes (Ed., Muller F.) Vol. 3, CRC Press, Boca Raton, FL, pp. 121–211.
Wittekind M., Görlach M., Friedrichs M.S., Dreyfuss G. and Müller L. (1992a) Biochemistry, 31, 6254–6265.
Wittekind M., Rajagopal P., Branchini B.R., Reizer J., Saier M.H. and Klevit R. (1992b) Protein Sci., 1, 1363–1376.
Wittekind m., Reizer J. and Klevit R.E. (1990) Biochemistry, 29, 7191–7200.
Wüthrich K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Eriksson, PO., Sahlman, L. 1H NMR studies of the mercuric ion binding protein MerP: Sequential assignment, secondary structure and global fold of oxidized MerP. J Biomol NMR 3, 613–626 (1993). https://doi.org/10.1007/BF00198367
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00198367