Mapping the structural basis for mechanistic diversity in metalloenzyme superfamilies
type: Grant
alternate name: 3R35GM119707-07S1
description: Project Summary The parent grant for this supplement aims to discover novel enzymatic cofactors involved in DNA biosynthesis in pathogens. The overarching goal is to enable new routes to enzyme inhibition in bacteria that cause infectious disease. Here we will investigate the mechanism of assembly of an essential tyrosine-derived post-translationally modified radical cofactor found in a subclass of microbial ribonucleotide reductases through incorporation of non- native amino acids. This approach will allow us to identify aspects of cofactor assembly that could be targeted for disruption by therapeutic interventions. In a second aim, we will characterize the cofactor used by this enzyme subclass in a native host organism. The project as a whole will set the stage for understanding how this enzyme subclass is used inside the cell, ultimately allow us to test the impact of disruption of cofactor assembly in a relevant biological context. The project provides an excellent training opportu
amount: MonetaryAmount
  value: 58746
  currency: USD
funder: NIH — NIH
funder alt: US National Institutes of Health
recipient: PENNSYLVANIA STATE UNIVERSITY, THE
start date: 2016-08-01
end date: 2026-05-31
license: https://creativecommons.org/publicdomain/zero/1.0/
source: https://reporter.nih.gov/project-details/10598851
source organization: NIH RePORTER
publisher: AI Analytics
keywords: R35
keywords: NIH
keywords: 3

AI Analytics
type: Organization