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Mercury-199 NMR of the Metal Receptor Site in MerR and Its Protein-DNA Complex

Utschig, Lisa M., Bryson, James W., O'Halloran, Thomas V.·1995·Science

Abstract

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 199 Hg 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.

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Metadata

Authors
Utschig, L. M., Bryson, J. W., & O'Halloran, T. V.
Venue
Science
Published
1995-04-21
Volume
268
Issue
5209
Pages
380-385
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2020081833
Cited by
183
References
0
FWCI
7.40
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Mercury-199 NMR of the Metal Receptor Site in MerR and Its Protein-DNA Complex. https://app.cochat.ai/papers/10.1126/science.7716541
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Utschig, L. M., Bryson, J. W., & O'Halloran, T. V. (1995). Mercury-199 NMR of the Metal Receptor Site in MerR and Its Protein-DNA Complex. Science. https://doi.org/10.1126/science.7716541

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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