High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.

  title={High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.},
  author={Joanne I. Yeh and H P Biemann and Gilbert G. Priv{\'e} and Jayvardhan Pandit and Daniel E. Koshland and S. H. Kim},
  journal={Journal of molecular biology},
  volume={262 2},
The high-resolution structures of the wild-type periplasmic domain of the bacterial aspartate receptor have been determined in the absence and presence of bound aspartate to 1.85 and 2.2 A resolution, respectively. As we reported earlier, in the refined structure of the complexed form of the crosslinked cysteine mutant receptor, the binding of the aspartate at the first site was mediated through four bridging water molecules while the second site showed an occupant electron density that best… 

Structural Analysis of the Ligand-Binding Domain of the Aspartate Receptor Tar from Escherichia coli.

  • T. Mise
  • Chemistry, Biology
  • 2016
To understand the molecular mechanisms underlying the induction of Tar activity by an attractant, the three-dimensional structures of the E. coli Tar periplasmic domain with and without bound aspartate, Asp-Tar and apo-Tar, respectively, were determined.

Mutations That Affect Ligand Binding to the Escherichia coli Aspartate Receptor

Results obtained for an alanine mutant were similar to those with cysteine and histidine mutants, indicating that side chain size was not an important factor here and that steric considerations are important here.

Hydrogen Exchange Reveals a Stable and Expandable Core within the Aspartate Receptor Cytoplasmic Domain*

The cytoplasmic domain is a flexible region poised for stabilization by small changes in electrostatic and hydrophobic interactions such as those caused by methylation of glutamate residues and by ligand-induced conformational changes during signaling.

Ligand Specificity Determined by Differentially Arranged Common Ligand-binding Residues in Bacterial Amino Acid Chemoreceptors Tsr and Tar*

It is proposed that all these Tsr- and Tar-specific features contribute to specific recognition of serine and aspartate with the arrangement of the side chain of residue 68 being the most critical.

A PAS Domain Binds Asparagine in the Chemotaxis Receptor McpB in Bacillus subtilis*

Results reveal not only a novelChemoreceptor sensing domain architecture but also, possibly, a different mechanism for chemoreceptor activation.

Cysteine and Disulfide Scanning Reveals a Regulatory α-Helix in the Cytoplasmic Domain of the Aspartate Receptor*

Interestingly, the rapid rates and promiscuous nature of disulfide formation reactions within the scanned region reveal that the cytoplasmic domain of the full-length, membrane-bound receptor has a highly dynamic structure.

Crystal Structure of a Functional Dimer of the PhoQ Sensor Domain*S⃞

The PhoP-PhoQ two-component system is a well studied bacterial signaling system that regulates virulence and stress response. Catalytic activity of the histidine kinase sensor protein PhoQ is

Identification of residues within ligand‐binding domain 1 (LBD1) of the Borrelia burgdorferi OspC protein required for function in the mammalian environment

The hypothesis that OspC interacts with a mammalian derived ligand that is critical for survival during early infection is supported and the hypothesis that LBD1 is a determinant of OSpC function in the mammalian environment is supported.