Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex.
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.
Utschig
L M
LM
Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.
Bryson
J W
JW
O'Halloran
T V
TV
D000495:Allosteric Site; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001483:Base Sequence; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008628:Mercury / Q000378:metabolism*; D008629:Mercury Isotopes; D008667:Metalloproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D011522:Protons; D013816:Thermodynamics
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C051124:MerR protein, Bacteria; D008629:Mercury Isotopes; D008667:Metalloproteins; D011522:Protons; D004247:DNA; D008628:Mercury