Structural Basis for the Selective Pb(II) Recognition of Metalloregulatory Protein PbrR691
Shanqing Huang, Xichun Liu, Dan Wang
1School of Life Sciences, Fudan University , Shanghai 200433, P. R. China.
Abstract:
The transcription regulator PbrR691, one of the MerR family proteins, shows extremely high sensitivity and selectivity toward Pb(II) in Ralstonia metallidurans CH34. Here, we present the crystal structure of PbrR691 in complex with Pb(II) at 2.0 Å resolution. The Pb(II) coordinates with three conserved cysteines and adopts a unique trigonal-pyramidal (hemidirected) geometry. To our knowledge, the PbrR691-Pb(II) structure provides the first three-dimensional visualization of a functional hemidirected lead(II) thiolate coordinate geometry in a protein.
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Regulation of the Unfolded Protein Response
Directing Proteins to the Rough Endoplasmic Reticulum
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Other Stress Responses in Bacteria
Valence Bond Theory


