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Science 21 April 1995:
Vol. 268. no. 5209, pp. 380 - 385
DOI: 10.1126/science.7716541
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Articles

Science, Vol 268, Issue 5209, 380-385
Copyright © 1995 by American Association for the Advancement of Science

articles

Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex

LM Utschig, JW Bryson, and TV O'Halloran

Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.

Structural insights have been provided by mercury-199 nuclear magnetic resonance (NMR) into the metal receptor site of the MerR metalloregulatory protein alone and in a complex with the regulatory target, DNA. The one- and two-dimensional NMR data are consistent with a trigonal planar Hg-thiolate coordination environment consisting only of Cys side chains and resolve structural aspects of both metal ion recognition and the allosteric mechanism. These studies establish 199Hg NMR techniques as useful probes of the metal coordination environment of regulatory proteins, copper enzymes, and zinc transcription factor complexes as large as 50 kilodaltons.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Mercury Resistance in Bacillus cereus RC607: Transcriptional Organization and Two New Open Reading Frames.
A. Gupta, L. T. Phung, L. Chakravarty, and S. Silver (1999)
J. Bacteriol. 181, 7080-7086
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Cd(II)-Responsive and Constitutive Mutants Implicate a Novel Domain in MerR.
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Metal Ion Chaperone Function of the Soluble Cu(I) Receptor Atx1.
R. A. Pufahl, C. P. Singer, K. L. Peariso, S. Lin, P. J. Schmidt, C. J. Fahrni, V. C. Culotta, J. E. Penner-Hahn, and T. V. O'Halloran (1997)
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