Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites.

The catalytic domain of protein tyrosine kinases can interconvert between active and inactive conformations in response to regulatory inputs. We recently demonstrated that Src kinase features an allosteric network that couples substrate-binding sites. However, the extent of conformational and dynamic changes that are propagated throughout the kinase domain remains poorly understood.

Thiolactomycin-based β-ketoacyl-AcpM synthase A (KasA) inhibitors: fragment-based inhibitor discovery using transient one-dimensional nuclear overhauser effect NMR spectroscopy.

Thiolactomycin (TLM) is a natural product inhibitor of KasA, the β-ketoacyl synthase A from Mycobacterium tuberculosis. To improve the affinity of TLM for KasA, a series of TLM analogs have been synthesized based on interligand NOEs between TLM and a pantetheine analog when both are bound simultaneously to the enzyme. Kinetic binding data reveal that position 3 of the thiolactone ring is a suitable position for elaboration of the TLM scaffold, and the structure-activity relationship studies provide information on the molecular features that govern time-dependent inhibition in this enzyme system.

SapT, a lanthionine-containing peptide involved in aerial hyphae formation in the streptomycetes.

The developmentally complex soil microbe Streptomyces tendae secretes a hydrophobic peptide that restored to developmental mutants of S. coelicolor the ability to raise aerial hyphae. The S.

Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9.

The stability of the isolated C-terminal domain of the ribosomal protein L9 (CTL9) is strongly dependent upon pH. Below pH 4.2, the folded and unfolded states are both populated significantly.