March 16–18, 2021
Poster Wall
Structure determination and identification of inhibitors against FmtA of Staphylococcus aureus
Dalal Vikram (Washington University St. Louis)
Description:
Staphylococcus aureus is one of the main causes of infections in hospitals and populations.
FmtA is known to remove D-Ala from Teichoic acids. We determined the crystal structure of FmtA. In
FmtA, the absence of a long loop I, interactions between Loop I and Ω-Loop, the folding of Loop II
over the active site, and the tilting of β12 and β13 strands results in the formation of solvent-exposed
and enlarged active site. Our study showed that Ser127 acts as a nucleophile, Lys130 performs the
acylation/deacylation, and Tyr211 plays a vital role in the binding of the substrate. Further,
we have screened active compounds and the binding affinity was confirmed using molecular docking
and Molecular dynamics simulation.
Discovery of Small-Molecule Inhibitors of the Bacterial Ribonuclease P
Alejandro Madrigal-Carrillo (UNAM)
Description:
RNase P is an essential ribonucleoprotein complex involved
in the biosynthesis of proteins in all organisms via the maturation
of all pre-tRNAs through the phosphodiester bond cleavage of its
5'-leader sequence. We consider the RNase P protein subunit as a
promising target for the discovery of antibiotics. We developed an
activity-binding-structure platform for screening compound libraries
based on a novel RNase P activity assay by fluorescence
spectroscopy, biolayer interferometry and synchrotron X-ray
diffraction analysis to search for the binding of small molecules to
the RNase P protein subunit and discovered a novel inhibitor, the
purpurin, which serves as a scaffold for structure-guided design of
future antibiotics.
Need Assistance?
Please contact the workshop coordinator if you have questions.
Mercy Baez
(631) 344-5769
(631) 344-7039
NSLS-II_MX_2021@bnl.gov
