Science · 1995 · 182 citations · 31 references
Natural SciencesBiochemistryMolecular BiologyMolecular BiophysicsStructural BiologyStructural BiophysicsBioinorganic ChemistryCoordination ChemistryLigand BindingMetal-ligand BondingProtein Complex AnalysisStructural Basis Of RecognitionEnzymesMetal CoordinationMetal Ion CoordinationMetal Ion Coordination SitesMetal-binding ProteinsTranscription Factor ComplexesTwo-dimensional Nmr SpectroscopyZinc Binding Proteins
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.
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DNA recognition by GAL4: structure of a protein-DNA complex
Ronen Marmorstein, Michael Carey, Mark Ptashne et al. · Nature · 1992 · 675 citations